3.4.21.4 (2R,4R)-4-phenyl-1-[Nalpha-(7-methoxy-2-naphthalenesulfonyl)-L-arginyl]-2-piperidinecarboxylic acid competitive, small molecular weight inhibitor without tryptase inhibitor activity 54138 3.4.21.4 (4-(6-chloro-naphthalene-2-sulfonyl)-piperazin-1-yl)-(3,4,5-6-tetrahydro[2H-1,4']bipyridinyl-4yl)-methanone - 117779 3.4.21.4 1,10-phenanthroline - 62 3.4.21.4 1-(L-trans-epoxysuccinyl-leucylamino)-4-guanidinobutane 6.09% inhibition at 0.1 mM 66433 3.4.21.4 1-(L-trans-epoxysuccinyl-leucylamino)-4-guanidinobutane 16.9% inhibition at 0.1 mM 66433 3.4.21.4 1-[N2-[(7-methoxynaphthalen-2-yl)sulfonyl]-L-arginyl]-4-phenylpiperidine-2-carboxylic acid IC50: 0.0003 mM 54139 3.4.21.4 2,7-bis(4-amidinobenzylidene)-cycloheptan-1-one - 22535 3.4.21.4 2,7-bis(4-amidinobenzylidene)cycloheptan-1-one unspecific strong inhibition 17264 3.4.21.4 2-mercaptoethanol 0.1 mM, isoenzyme aT-I loses 90% of its activity, isoenzyme aT-II loses 93% of its activity 63 3.4.21.4 3,4-dichloroisocoumarin - 1040 3.4.21.4 4-(2-aminoethyl)-benzensulfonylfluoride isozyme TryIII activity is completely (more than 95%) inhibited by 4-(2-aminoethyl)-benzensulfonylfluoride 151539 3.4.21.4 4-(amidinophenyl)methanesulfonyl fluoride - 132464 3.4.21.4 6-amidino-2-naphthol mixed-type inhibition 117777 3.4.21.4 acetonitrile partial inhibition at 20% acetonitrile, a 5% aqueous acetonitrile solution less likely reduces the activity of the porous polymer monolith-immobilized trypsin 981 3.4.21.4 acyclic SFTI i.e. oSFTI, modified sunflower trypsin inhibitor 1, SFTI-1, generated by Fmoc-based automated synthesis 80780 3.4.21.4 acyclic sun flower trypsin inhibitor-1 - 151553 3.4.21.4 Adenanthera pavonina trypsin inhibitor i.e. ApTI, isolated and purified from seeds, retards larval and pupal developmental and growth of larvae of Anticarsia gemmatalis, overview 15014 3.4.21.4 Adenanthera pavonina trypsin inhibitor i.e. ApTI, isolated and purified from seeds, retards larval and pupal developmental and growth of Corcyra cephalonica, overview 15014 3.4.21.4 Adenanthera pavonina trypsin inhibitor i.e. ApTI, isolated and purified from seeds, retards larval and pupal developmental and growth of Diatraea saccharalis, overview 15014 3.4.21.4 Adenanthera pavonina trypsin inhibitor i.e. ApTI, isolated and purified from seeds, retards larval and pupal developmental and growth of Anagasta kuehniella, a severe pest in flour mills, at 1% with a significant reduction in larval survival and weight, effects of this inhibitor on food consumption, absorption and utilization, as well as the effects of the inhibitor on the midgut proteolytic activity of larvae fed on an artificial diet, overview 15014 3.4.21.4 Adenanthera pavonina trypsin inhibitor i.e. ApTI, isolated and purified from seeds, has only slight retarding effect on larval and pupal developmental and growth of Sitotroga cerealella, overview 15014 3.4.21.4 Adenanthera pavonina trypsin inhibitor i.e. ApTI, isolated and purified from seeds, retards larval and pupal developmental and growth of Spodoptera frugiperda, overview 15014 3.4.21.4 Adunil CEL 0.1% v/v, 47.3% residual activity 201663 3.4.21.4 alpha-1-antitrypsin in gestational diabetes mellitus reduction of serum trypsin inhibitory capacity may be due to non-enzymatic glycosylation of alpha-1-antitrypsin or oxidation of methionine in the active site of alpha-1-antitrypsin 5266 3.4.21.4 alpha1-antitrypsin - 1571 3.4.21.4 alpha1-antitrypsin Pittsburgh effective inhibitor, variant of alpha1-antitrypsin containing an Arg residue in place of the P1 Met358 in the reactive-site peptide bond 139023 3.4.21.4 antipain IC50: 0.04 mM 520 3.4.21.4 antipain 0.01 mM, isoenzyme aT-I loses 96% of its activity, isoenzyme aT-II loses 99% of its activity 520 3.4.21.4 Apios Americana trypsin inhibitor AATI, strong inhibitor, complete inhibition with Apios Americana trypsin inhibitor bound to trypsin in a 1:2 molar ratio 75354 3.4.21.4 Aprotinin - 405 3.4.21.4 Aprotinin very efficient inhibition of trypsin-1 and trypsin-2, but not of trypsin-4 405 3.4.21.4 Aprotinin immobilized enzyme 405 3.4.21.4 atropine strongly diminishes trypsin activity in stressed animals 4789 3.4.21.4 AVNIPFKVHFRCKAAFC a small trypsin inhibitor from the skin secretion of the frog Odorrana grahami, only inhibits the hydrolysis activity of trypsin on synthetic chromogenic substrate 75353 3.4.21.4 Ba2+ 27% inhibition at 5 mM 111 3.4.21.4 Ba2+ - 111 3.4.21.4 Bauhinia variegata var. variegata trypsin inhibitor i.e. BvvTI, a Kunitz-type inhibitor from seeds of the Camel’s foot tree, Bauhinia variegata var. variegata. The inhibitor is also capable of significant inhibition of the proliferation of nasopharyngeal cancer CNE-1 cells in a selective way and of inhibiting anti-HIV-1 reverse transcriptase activity, overview 159910 3.4.21.4 benzamidine - 579 3.4.21.4 benzamidine unspecific, weak inhibition 579 3.4.21.4 benzamidine 1 mM, isoenzyme aT-I loses 90% of its activity, isoenzyme aT-II loses 93% of its activity 579 3.4.21.4 benzamidine complete inhibition 579 3.4.21.4 benzamidine 5 mM, 22% residual activity 579 3.4.21.4 benzamidine competitive inhibitor 579 3.4.21.4 benzamidine 99% inhibition at 1 mM 579 3.4.21.4 benzamidine 55% inhibition at 5 mM 579 3.4.21.4 benzamidine 54% inhibition at 5 mM 579 3.4.21.4 benzamidine 72.0% inhibition of trypsin A, 95.4% of trypsin B, at 1 mM. 88.8% inhibition of trypsin A, 97.6% of trypsin B at 0.1 mM, 579 3.4.21.4 benzamidine 5 mM, 17.9% residual activity 579 3.4.21.4 benzamidine 80.2% inhibition 579 3.4.21.4 benzylamine - 529 3.4.21.4 benzyloxycarbonyl-amino(4-guanidinophenyl)methyl-bis(4-ethylphenyl)phosphonate 50% inhibition at 0.000017 mM, comparison with inhibitory effect on urokinase 131779 3.4.21.4 benzyloxycarbonyl-amino(4-guanidinophenyl)methyl-bis(4-isopropylphenyl)phosphonate 50% inhibition at 0.000061 mM, comparison with inhibitory effect on urokinase 131780 3.4.21.4 benzyloxycarbonyl-amino(4-guanidinophenyl)methyl-bis(4-methylthiophenyl)phosphonate 50% inhibition at 0.0000087 mM, comparison with inhibitory effect on urokinase 131782 3.4.21.4 benzyloxycarbonyl-amino(4-guanidinophenyl)methyl-bis(4-t-butylphenyl)phosphonate 50% inhibition at 0.000088 mM, comparison with inhibitory effect on urokinase 131781 3.4.21.4 bis(m-amidinosalicylidene-L-alaninato)iron(III) - 54137 3.4.21.4 bis(p-amidinosalicylidene-L-alaninato)iron(III) - 54136 3.4.21.4 bisphenol A the secondary and tertiary structures of trypsin are altered by bisphenol S binding, which results in the loosening of the skeleton of the enzyme. Bisphenol S induces microenvironmental changes around tyrosine and tryptophan residues of trypsin. The activity of trypsin does not change remarkably with the increasing concentration of bisphenol S. The binding of bisphenol S to trypsin is a spontaneous process and hydrogen bonding and hydrophobic interactions play a vital role in stabilizing the bisphenol S-trypsin complex. The binding constants of bisphenol S with trypsin are 74200 (25°C) and 59100 L/mol (37°C) 3723 3.4.21.4 black gram trypsin inhibitor 1 highly effective trypsin inhibitor, 87.5% of trypsin inhibitory activity of black gram trypsin inhibitor 1 is retained after treatment with 10 mM dithiothreitol for 2 hours, and the activity dwindles to 12.5% after treatment with 100 mM dithiothreitol for 2 hours 151560 3.4.21.4 black gram trypsin inhibitor 2 highly effective trypsin inhibitor, the trypsin inhibitory activity of black gram trypsin inhibitor 2 is unaffected after exposure to 100 mM dithiothreitol for 2 hours 151561 3.4.21.4 black gram trypsin inhibitor 3 highly effective trypsin inhibitor, in the presence of 10 mM dithiothreitol trypsin inhibitory of black gram trypsin inhibitor 3 drops to 57.1% after 1 h and becomes undetectable after 2 hours, while treatment of 100 mM dithiothreitol for 1 h has the same effect 151562 3.4.21.4 Bovine pancreatic trypsin inhibitor - 2774 3.4.21.4 Bovine pancreatic trypsin inhibitor BPTI, a natural non-specific serine protease inhibitor which possesses the ability to inhibit trypsin, the inhibitory activity of recombinant BPTI against trypsin is the same as natural BPTI, the trade name is aprotinin 2774 3.4.21.4 Bovine pancreatic trypsin inhibitor BPTI 2774 3.4.21.4 Bovine pancreatic trypsin inhibitor also known as aprotinin. At the lowest aprotinin concentration of 0.000625 mg, the residual trypsin obtained in neonate larvae of shoot borer, internode borer and top borer is 33.6, 24.8 and 9.3%, respectively. The residual trypsin for third instar of shoot borer, internode borer and top borer at the lowest aprotinin concentration of 0.000125 mg is 55.0, 65.0 and 20.7%, respectively. The amount of aprotinin needed to bring about 50% inhibition of gut proteinases of third instar larvae is 0.00025 mg for shoot borer and 0.0025 mg for internode borer whereas 0.000125 mg is sufficient to bring about nearly 80% inhibition in top borer. 2774 3.4.21.4 Bovine pancreatic trypsin inhibitor i.e. BPTI or aprotinin, influence of temperature on the relationship between structure and dynamics of the inhibitor protein, calculations and X-ray crystal structure of BPTI at 1.5 A resolution, global diffusion and internal motions, overview 2774 3.4.21.4 bovine secretory inhibitors A and B 102575 3.4.21.4 Bowman-Birk inhibitor double-headed native trypsin/chymotrypsin inhibitor in soybeans, which inhibits trypsin and chymotrypsin in a non-competitive manner, 78% reduced activity in the presence of 0.0005 mM Bowman-Birk inhibitor 17259 3.4.21.4 Bowman-Birk inhibitor - 17259 3.4.21.4 BPTI-20st simplified variant of bovine pancreatic trypsin inhibitor containing 20 alanines, retains a wild type level of trypsin inhibitory activity 151558 3.4.21.4 BPTI-[5,55]st single-disulfide-bonded variant of bovine pancreatic trypsin inhibitor, retains a wild type level of trypsin inhibitory activity 151559 3.4.21.4 captopril feeding angiotensin converting enzyme inhibitor captopril down-regulates trypsin activity in the larval gut, injecting third instar larvae with a combination of Aedes aegypti trypsin-modulating oostatic factor and captopril downregulates trypsin biosynthesis in the larval gut 469 3.4.21.4 Cd2+ 10 mM, 48% inhibition 52 3.4.21.4 chymostatin - 511 3.4.21.4 clispin a Clitocybe nebularis trypsin inhibitor variant, recombinantly expressed in Escherichia coli, highly specific towards trypsin, fast-acting, and tight-binding. Molecular cloning of the gene and cDNA encoding cnispin, overview 80778 3.4.21.4 Clitocybe nebularis trypsin inhibitor CnSPI, several inhibitor variants, separation by trypsin affinity chromatography. Possible regulatory role for CnSPIs in the endogenous proteolytic system of Clitocybe nebularis. Isolation from frozen fruiting bodies or basidiocarps 159920 3.4.21.4 cMCoTI-II - 80782 3.4.21.4 Co2+ 48% inhibition at 5 mM 23 3.4.21.4 Co2+ - 23 3.4.21.4 Co2+ 10 mM, 31.6% inhibition 23 3.4.21.4 CRC 220 - 33650 3.4.21.4 Cu2+ 14% inhibition at 5 mM 19 3.4.21.4 Cu2+ 68% inhibition at 5 mM 19 3.4.21.4 Cu2+ - 19 3.4.21.4 cyclic SFTI i.e. cSFTI, modified sunflower trypsin inhibitor 1, SFTI-1, generated by Fmoc-based automated synthesis 80779 3.4.21.4 DFP - 923 3.4.21.4 dithiothreitol 1 mM, no residual activity 45 3.4.21.4 DMTI-II trypsin inhibitor from seeds of Dimorphandra mollis. The inhibitory activity is stable over a wide range and in the presence of DTT 54140 3.4.21.4 domesticated soybean inhibitor SBTI 151555 3.4.21.4 DOTA-SFTI modified sunflower trypsin inhibitor 1, SFTI-1, labeled, generated by Fmoc-based automated synthesis 80781 3.4.21.4 E-64 18.3% inhibition of trypsin A, 11.1% of trypsin B, at 0.001 mM. 46.9% inhibition of trypsin A, 33.8% of trypsin B at 0.01 mM 559 3.4.21.4 E-64 0.02 mM, 19.5% residual activity 559 3.4.21.4 E64 weak inhibition 1457 3.4.21.4 Ecballium elaterium trypsin inhibitor II EETI, a a model member of the knottin family, used for construction of libraries of EETI loop-substituted variants with diversity in both amino acid sequence and loop length, wild-type EETI or loop-substituted clones expressed from yeast, structure-function analysis, modelling, overview 159926 3.4.21.4 EDTA 50 mM, 88% residual activity 21 3.4.21.4 EDTA 6.85% inhibition at 2 mM 21 3.4.21.4 EDTA weak inhibition, 18% inhibition at 10 mM 21 3.4.21.4 EDTA 12% inhibition at 5 mM 21 3.4.21.4 EDTA 10% inhibition at 2 mM 21 3.4.21.4 EDTA a metalloenzyme inhibitor, 8% inhibition at 5 mM 21 3.4.21.4 EDTA 14.2% inhibition at 2 mM 21 3.4.21.4 EDTA 1 mM, 53.9% residual activity 21 3.4.21.4 EDTA - 21 3.4.21.4 enalapril feeding angiotensin converting enzyme inhibitor enalapril down-regulates trypsin activity in the larval gut 3286 3.4.21.4 ethylenediaminetetraacetic acid partial 10903 3.4.21.4 Gly-L-Arg-(2-amino butanoyl)-L-Thr-Nphe-L-Ser-L-Ile-L-Pro-L-Pro-L-Ile-(2-amino butanoyl)-L-Phe-L-Pro-L-Asp - 151546 3.4.21.4 Gly-L-Arg-L-Cys-L-Thr-L-Lys-L-Ser-L-Ile-L-Pro-L-Pro-L-Ile-L-Cys-L-Phe-L-Pro-L-Asp sun flower trypsin inhibitor SFTI-1 151544 3.4.21.4 Glycine max trypsin inhibitor from raw soymilk, inhibition kinetics, overview 159924 3.4.21.4 Hg2+ 72% inhibition at 5 mM 33 3.4.21.4 Hg2+ 57% inhibition at 5 mM 33 3.4.21.4 Hg2+ strong inhibition 33 3.4.21.4 Hg2+ 10 mM, 85.7% inhibition 33 3.4.21.4 Hg2+ - 33 3.4.21.4 HgCl2 - 110 3.4.21.4 I-ovalbumin high affinity interaction of enzyme with I-ovalbumin, the product of a heating transition of ovalbumin which acts as a potent reversible serine proteinase inhibitor. Interaction is characterized by high kinetic association constants and low kinetic dissociation konstants 132463 3.4.21.4 iodoacetic acid 16.5% inhibition at 1 mM; 1 mM, 16.5% inhibition 213 3.4.21.4 K+ 10 mM, 16% inhibition 39 3.4.21.4 Kunitz domain 1 of tissue factor pathway inhibitor-2 - 60782 3.4.21.4 Kunitz type trypsin inhibitor from Glycine max isolated and purified from Korean large black soybeans cultivar, overview. Inhibits bovine trypsin, but also shows Anti-HIV reverse transcriptase activity, cytokine-inducing activity and antiproliferative activity on tumor cell lines 159923 3.4.21.4 L-1-chloro-3-tosylamido-4-phenyl-2-butanone - 93760 3.4.21.4 L-1-chloro-3-[4-tosylamido]-4-phenyl-2-butanone - 44286 3.4.21.4 L-Lys-L-Cys-L-Thr-Nlys-L-Ser-L-Ile-L-Pro-L-Pro-L-Ile-L-Cys-L-Phe-L-Pro-L-Asp - 151545 3.4.21.4 leech-derived tryptase inhibitor i.e. LDTI, purely competitive inhibitor 117784 3.4.21.4 LEKTI the LEKI gene encodes a 15-domain serine proteinase inhibitor, disulfide bonds are important for LEKTI function, noncompetitive mechanism, expression and purification of human LEKTI gene in Sf9 11354 3.4.21.4 leupeptin IC50: 0.0002 mM 217 3.4.21.4 leupeptin 0.1 mM, isoenzyme aT-I loses 97% of its activity, isoenzyme aT-II completely loses its activity 217 3.4.21.4 leupeptin - 217 3.4.21.4 Li+ 10 mM, 19% inhibition 152 3.4.21.4 lily bulb trypsin inhibitor - 75361 3.4.21.4 Lima bean trypsin inhibitor - 6678 3.4.21.4 Lima bean trypsin inhibitor 0.002 mM, 7.9% residual activity 6678 3.4.21.4 LKGCWTKSIPPKPCFGK - 151541 3.4.21.4 Locusta migratoria protease inhibitor 1 strong inhibition 151543 3.4.21.4 Locusta migratoria protease inhibitor 3 strong inhibition, the inhibitor interacts with trypsin through the reactive site P3-P4' and the P10-P6 residues 151542 3.4.21.4 low-molecular-mass trypsin inhibitor inhibitor type-2 from Sinapis alba, inhibitor consists of a peptide mixture, displaying Ile or Arg at position 43, Trp or kynurenine at position 44, and C-terminal ragged ends 117776 3.4.21.4 m-amidinosalicylidene-L-alaninato(aqua)copper(II) - 54135 3.4.21.4 m-amidinosalicylidene-L-alaninato(aqua)copper(II) hydrochloride - 159914 3.4.21.4 m-guanidinosalicylidene-L-alaninato(aqua)copper(II) - 159912 3.4.21.4 Mg2+ 24% inhibition at 5 mM 6 3.4.21.4 Mg2+ 10 mM, 21.6% inhibition 6 3.4.21.4 Mn2+ 34.5% inhibition at 5 mM 11 3.4.21.4 Mn2+ - 11 3.4.21.4 additional information naturally occurring trypsin inhibitor SFTI-1 isolated from sunflower seeds and its analogues 2 3.4.21.4 additional information 4-guanidinebenzoate: no inhibition up to 0.2 mM 2 3.4.21.4 additional information not inhibitory: EDTA, tosyl-L-Phe chloromethyl ketone 2 3.4.21.4 additional information not inhibitory: Ca2+ up to 500 mM 2 3.4.21.4 additional information not inhibitory: chymostatin 2 3.4.21.4 additional information trypsin 4 is completely resistant to chymotryptic degradation 2 3.4.21.4 additional information not inhibited by 1-(L-trans-epoxysuccinyl-leucylamino)-4-guanidinobutane, N-ethylmaleimide, iodoacetic acid, N-tosyl-L-phenyl-alanine-chloromethyl ketone, and pepstatin 2 3.4.21.4 additional information mesotrypsin exhibits complete resistance against wild-type alpha1-antitrypsin 2 3.4.21.4 additional information 1-(L-trans-epoxysuccinyl-leucylamino)-4-guanidinobutane, N-ethylmaleimide, iodoacetic acid, chymotrypsin, pepstatin A, and EDTA have no inhibitory effect 2 3.4.21.4 additional information notinhibited by pepstatin A 2 3.4.21.4 additional information resistant to soybean trypsin inhibitor and aprotinin 2 3.4.21.4 additional information trypsin is not inhibited by N-(4-aminobutyl)-L-Arg-L-Cys-L-Thr-L-Lys-L-Ser-L-Ile-L-Pro-L-Pro-L-Ile-L-Cys-L-Phe-L-Pro-L-Asp and N-benzylglycine-L-Arg-L-Cys-L-Thr-L-Lys-L-Ser-L-Ile-L-Pro-L-Pro-L-Ile-L-Cys-L-Phe-L-Pro-L-Asp 2 3.4.21.4 additional information trypsin activity decreases with age, trypsin activity correlates inversely with cholesterol concentration and plasmin and elastase activity 2 3.4.21.4 additional information aspartate (PepA) and cysteine (E64) protease inhibitors as well as the chymotrypsin inhibitor tosyl-L-phenylalanine chloromethylketone have no effect on enzymatic activity of isozyme TryIII 2 3.4.21.4 additional information not inhibited by up to 0.05 mM SVIGCWTFSIPPRPCFVK-amide 2 3.4.21.4 additional information trypsin is not inhibited by N-(4-aminobutyl)-L-Arg-L-Cys-L-Thr-L-Lys-L-Ser-L-Ile-L-Pro-L-Pro-L-Ile-L-Cys-L-Phe-L-Pro-L-Asp and N-benzylglycine-L-Arg-L-Cys-L-Thr-L-Lys-L-Ser-L-Ile-L-Pro-L-Pro-L-Ile-L-Cys-L-Phe-L-Pro-L-Asp, Gly-L-Arg-(2-amino butanoic acid)-L-Thr-Nlys-L-Ser-L-Ile-L-Pro-L-Pro-L-Ile-(2-amino butanoyl)-L-Phe-L-Pro-L-Asp, L-Lys-(2-amino butanoyl)-L-Thr-Nlys-L-Ser-L-Ile-L-Pro-L-Pro-L-Ile-(2-amino butanoyl)-L-Phe-L-Pro-L-Asp, and Nlys-(2-amino butanoyl)-L-Thr-Nlys-L-Ser-L-Ile-L-Pro-L-Pro-L-Ile-(2-amino butanoyl)-L-Phe-L-Pro-L-Asp 2 3.4.21.4 additional information the crude and partially purified extract from Passiflora f. edulis flavicarpa leaves displays inhibitory effect towards trypsin, methyl jasmonate treatment of the leaves increases the inhibitory activity against trypsin 2 3.4.21.4 additional information no inhibition by N-alpha-tosyl-L-Phe-chloromethyl ketone, E-64, and O-fenantroline 2 3.4.21.4 additional information identification of trypsin-3 binding peptides, and molecular modeling of the binding of peptides to isozyme trypsin-3. The degradation rate of peptides by trypsin correlates to their inhibitory efficacy, the most stable peptides being the most effective inhibitors, overview 2 3.4.21.4 additional information design and synthesis of Schiff base metal chelate inhibitors of trypsin, structural basis, overview. The binding mode of the guanidino groups of m-guanidinosalicylidene-L-alaninato(aqua)copper(II) hydrochloride and [N,N'-bis(m-guanidinosalicylidene)ethylenediaminato]copper(II) to Asp189 in the S1 pocket of trypsin is markedly different from of the amidino group of m-amidinosalicylidene-L-alaninato(aqua)copper(II) hydrochloride. The active site residues of trypsin play a crucial role in the binding affinity to the trypsin molecule. 2 3.4.21.4 additional information no inhibition by EDTA, E-64, and pepstatin A 2 3.4.21.4 additional information no or poor inhibition by pepstatin A, 2-mercaptoethanol, Ca2+, K+, and Na+ 2 3.4.21.4 additional information no inhibition by pepstatin A, 2-mercaptoethanol and EDTA 2 3.4.21.4 additional information no or poor inhibition by E-64, N-ethylmaleimide, iodoacetic acid, TPCK, pepstatin A, and EDTA 2 3.4.21.4 additional information the enzyme activity is completely stable in presence of detergents, overview. No inhibition by EDTA, 2-nercaptoethanol, pepstatin A, Ca2+, Ba2+, Zn2+, Cu2+, Mg2+, Mn2+, K+, and Na+ 2 3.4.21.4 additional information no or poor inhibition by N-tosyl-L-phenylalanine chloromethylketone, EDTA, 2-mercaptoethanol, pepstatin A, iodoacetic acid, and E-64 2 3.4.21.4 additional information no inhibition by E-64, N-ethylmaleimide, iodoacetic acid, pepstatin A, and Nalpha-4-tosyl-L-Phe-chloromethylketone 2 3.4.21.4 additional information no or poor inhibition by pepstatin A, EDTA, 2-mercaptoethanol, and N-p-tosyl-L-phenylalanine chloromethyl ketone 2 3.4.21.4 additional information determination of serum trypsin inhibitory capacity of plasma in psoriatic patients, which is increased compared to healthy persons 2 3.4.21.4 additional information inhinitory potencies of the different legume trypsin inhibitors, overview 2 3.4.21.4 additional information infection of Lutzomyia longipalpis with Leishmania mexicana reduces trypsin-like activity in the sand fly midgut, overview 2 3.4.21.4 additional information no or poor inhibition of trypsin A and trypsin B by pepstatin at 0.001 mM, and EDTA and 1,10-phenathroline at 10 mM 2 3.4.21.4 additional information no inhibition by DTNB and 2-mercaptoethanol 2 3.4.21.4 additional information no inhibition by N-ethylmaleimide 2 3.4.21.4 additional information effective inhibition of the catalytic activity by metal ions observed in trypsin R96H is caused by specific and reversible reorganization of the active site in the enzyme 2 3.4.21.4 mung bean trypsin inhibitor synthesis and inhibitory activity of mutant inhibitor variants expressed in Escherichia coli, overview 159917 3.4.21.4 mung bean trypsin inhibitor 0.003 mM, 3.6% residual activity 159917 3.4.21.4 mustard trypsin inhibitor 2 - 39041 3.4.21.4 mustard trypsin inhibitor 2 80% of trypsin activity can be inhibited by 42 nM mustard trypsin inhibitor 2 39041 3.4.21.4 mustard trypsin inhibitor II inhibition of HzTrypsin-C, no inhibition of HzTrypsin-S 117774 3.4.21.4 N-alpha-p-tosyl-L-lysine chloromethyl ketone 85.4% inhibition 13070 3.4.21.4 N-alpha-p-tosyl-L-lysine chloromethyl ketone 10 mM, 99.67% inhibition 13070 3.4.21.4 N-alpha-tosyl-L-Lys-chloromethyl ketone complete inhibition at 1 mM 159911 3.4.21.4 N-alpha-tosyl-L-lysine chlormethylketone less than 50% inhibition of isozyme TryIII by the trypsin-specific inhibitor N-alpha-tosyl-L-lysine chlormethylketone 151540 3.4.21.4 N-alpha-tosyl-L-lysine chloromethyl ketone - 94254 3.4.21.4 N-alpha-tosyl-L-lysine-chloromethylketone complete inhibition at 5 mM 159925 3.4.21.4 N-p-tosyl-L-lysine chloromethyl ketone complete inhibition at 5 mM 25027 3.4.21.4 N-p-tosyl-L-lysine chloromethyl ketone 89% inhibition at 0.1 mM 25027 3.4.21.4 N-p-tosyl-L-lysine chloromethyl ketone 88% inhibition at 5 mM 25027 3.4.21.4 N-p-tosyl-L-lysine chloromethyl ketone 5 mM, 83% inhibition 25027 3.4.21.4 N-p-tosyl-lysine chloroketone - 24081 3.4.21.4 N-tosyl-L-lysine chloromethyl ketone 82.9% inhibition at 5 mM 8472 3.4.21.4 N-tosyl-L-lysine-chloromethyl ketone complete inhibition 35487 3.4.21.4 N-tosyl-L-lysine-chloromethyl ketone 82% inhibition at 5 mM 35487 3.4.21.4 N-tosyl-L-phenyl-alanine-chloromethyl ketone 11% inhibition at 1mg/ml 139021 3.4.21.4 N-tosyl-L-phenylalanine-chloromethyl ketone 5.34% inhibition at 5 mM 66434 3.4.21.4 Na+ 10 mM, 21% inhibition 59 3.4.21.4 Na-p-tosyl-L-lysine chloromethyl ketone hydrochloride inhibits trypsin specifically and irreversibly, 40% reduced activity in the presence of 1 mM Na-p-tosyl-L-lysine chloromethyl ketone hydrochloride 151549 3.4.21.4 NaCl activity decreases with increasing NaCl concentrations (0-30%) 42 3.4.21.4 NaCl exhibits a progressive decrease in activity with increasing NaCl concentration (0-30%) 42 3.4.21.4 NaCl 60& inhibition at 35% NaCl 42 3.4.21.4 NaCl 60% inhibition at 30% NaCl 42 3.4.21.4 NaCl enzyme activity continuously decreases with increasing NaCl concentration of 0-30% 42 3.4.21.4 NaCl enzyme activity continuously decreases to 50% of maximal activity with increasing NaCl concentration of 0-30% 42 3.4.21.4 NaCl relative activities of trypsin isozymes A, B, and C at 15% NaCl are approximately 39%, 38% and 40% of maximal activity, respectively 42 3.4.21.4 NaCl 69% inhibition at 0.6 M 42 3.4.21.4 NaCl trypsin activity decreases continuously as NaCl concentration increases from 0–30% 42 3.4.21.4 Nafamostat potent inhibitor 11353 3.4.21.4 nafamostat mesilate IC50: 0.00003 mM 33735 3.4.21.4 Nalpha-(2-naphthylsulfonyl)-L-3-amidino-phenylalanine-4'-acetyl-piperazide - 53161 3.4.21.4 Nalpha-(2-naphthylsulfonyl)-L-3-amidino-phenylalanine-4'-methylpiperidide - 53155 3.4.21.4 Nalpha-(2-naphthylsulfonyl)-L-3-amidino-phenylalanine-D-pipecolic acid - 53156 3.4.21.4 Nalpha-(2-naphthylsulfonyl)-L-3-amidino-phenylalanine-D-pipecolic acid methyl ester - 53157 3.4.21.4 Nalpha-(2-naphthylsulfonyl)-L-3-amidino-phenylalanine-isopecotinic acid - 53158 3.4.21.4 Nalpha-(2-naphthylsulfonyl)-L-3-amidino-phenylalanine-isopecotinic acid methylester - 53159 3.4.21.4 Nalpha-(2-naphthylsulfonyl)-L-3-amidino-phenylalanine-piperazide - 53160 3.4.21.4 Nalpha-p-tosyl-L-lysine chloromethyl ketone complete inhibition 9443 3.4.21.4 Nalpha-tosyl-L-Lys-chloromethyl ketone - 11629 3.4.21.4 Nalpha-tosyl-L-Lys-chloromethyl ketone 91% inhibition at 1 mM 11629 3.4.21.4 Nalpha-tosyl-L-Lys-chloromethylketone - 40384 3.4.21.4 Nalpha-tosyl-L-Lys-chloromethylketone 79% inhibition at 5 mM 40384 3.4.21.4 Nalpha-tosyl-L-Lys-chloromethylketone 89% inhibition at 5 mM 40384 3.4.21.4 Nalpha-tosylglycyl-3-amidino-DL-phenylalanine-methyl ester - 22536 3.4.21.4 napsagatran - 16388 3.4.21.4 napsagatran ethylester - 53162 3.4.21.4 nexin-1 nexin-1 inhibits isozymes trypsin-1 ad trypsin-2, nexin-1 inhibits trypsin-4 and forms stable complexes only with this trypsin isoenzyme 75358 3.4.21.4 oMCoTI-II - 80783 3.4.21.4 ovomucoid - 4087 3.4.21.4 ovomucoid chicken ovomucoid 4087 3.4.21.4 p-amidinosalicylidene-L-alaninato(aqua)copper(II) - 54134 3.4.21.4 p-nitrophenyl-p'-guanidino-benzoate irreversible trypsin inhibitor 70941 3.4.21.4 p-tosyl-L-Lys-chloromethane - 47437 3.4.21.4 p-tosyl-L-Lys-chloromethane reaction towards B chain of insulin is inhibited, the activity towards the A-chain is not significantly affected 47437 3.4.21.4 pancreatic secretory trypsin inhibitor also known as serine protease inhibitor Kazal type 1 75357 3.4.21.4 pancreatic secretory trypsin inhibitor a Kazal-type specific trypsin inhibitor with narrow specificity for the inhibition of trypsin, with very little or no inhibitory capacity against other serine proteinases, even those exhibiting trypsin-like specificity 75357 3.4.21.4 Pancreatic trypsin inhibitor i.e. trasylol, kallikrein inactivator 16311 3.4.21.4 Pancreatic trypsin inhibitor bovine pancreatic trypsin inhibitor 16311 3.4.21.4 PdKI-3.1 isolation of two highly pH- and thermo-stable Kunitz-type inhibitors of trypsin from seeds of the tree Pithecellobium dumosum, overview 40382 3.4.21.4 PdKI-3.2 isolation of two highly pH- and thermo-stable Kunitz-type inhibitors of trypsin from seeds of the tree Pithecellobium dumosum, overview 40383 3.4.21.4 pefabloc - 2236 3.4.21.4 Pefabloc SC completely inhibits isoenzymes trypsin-1, trypsin-2, and trypsin-4 5680 3.4.21.4 Pefabloc SC complete inhibition of trypsin A and B at 1 mM 5680 3.4.21.4 Pefabloc SC 1 mM, 4.5% residual activity 5680 3.4.21.4 pepstatin - 396 3.4.21.4 pepstatin A 26% inhibition at 0.01 mM 309 3.4.21.4 Phaseolus vulgaris trypsin inhibitor two different variants of 132 kDa and 118 kDA from navy beans and red kidney beans, respectively, isolated by heat treatment and ammonium sulfate fractionation 159918 3.4.21.4 phenyl methyl sulphonyl fluoride 100% inhibition 159526 3.4.21.4 phenylbutylamine - 8511 3.4.21.4 Phenylethylamine - 900 3.4.21.4 phenylmethyl sulfonyl fluoride - 9370 3.4.21.4 phenylmethylsulfonyl fluoride - 257 3.4.21.4 phenylmethylsulfonyl fluoride partial 257 3.4.21.4 phenylmethylsulfonyl fluoride 5 mM, 43% residual activity 257 3.4.21.4 phenylmethylsulfonyl fluoride a serine protease inhibitor, over 90% inhibition of trypsin isozymes A, B and C at 5 mM 257 3.4.21.4 phenylmethylsulfonyl fluoride 10 mM, 4.5% residual activity 257 3.4.21.4 phenylmethylsulfonyl fluoride 100 mM, complete inhibition 257 3.4.21.4 Phenylmethylsulfonylfluoride - 1148 3.4.21.4 Phenylmethylsulfonylfluoride 89.5% inhibition at 1 mM 1148 3.4.21.4 Phenylpropylamine - 45829 3.4.21.4 Plathymenia foliolosa trypsin inhibitor PFTI 75356 3.4.21.4 PMSF 0.1 mM, isoenzyme aT-I loses 89% of its activity, isoenzyme aT-II loses 80% of its activity 248 3.4.21.4 PMSF 73% inhibition at 1 mM 248 3.4.21.4 PMSF - 248 3.4.21.4 PMSF complete inhibition 248 3.4.21.4 PMSF 62% inhibition at 1 mM, complete inhibition at 5 mM 248 3.4.21.4 PMSF 61% inhibition at 1 mM, complete inhibition at 5 mM 248 3.4.21.4 PMSF 80% inhibition at 1 mM, complete at 5 mM 248 3.4.21.4 PMSF 89% inhibition at 5 mM 248 3.4.21.4 PMSF 80.7% inhibition of trypsin A, 57.4% of trypsin B at 0.1 mM. 96.4% inhibition of trypsin A, 93.2% of trypsin B at 1 mM 248 3.4.21.4 polylysine immobilized enzyme 2581 3.4.21.4 porcine secretory inhibitors - 101335 3.4.21.4 porcine trypsin inhibitor 0.01 mM, more than 95% inhibition 201664 3.4.21.4 potato inhibitor II strong inhibition of HzTrypsin-C, no inhibition of HzTrypsin-S 117773 3.4.21.4 Protease Inhibitor Cocktail - 151547 3.4.21.4 Putranjiva roxburghii trypsin inhibitor highly potent inhibitor of bovine trypsin, trypsin inhibitory activity of Putranjiva roxburghii trypsin inhibitor is completely retained up to 70°C, above 70°C, there is a slight decrease in the inhibitory activity retaining almost 85% inhibitory activity up to 80°C, the inhibitory activity of Putranjiva roxburghii trypsin inhibitor falls sharply above 80°C with a loss of almost 80% inhibitory activity at 90°C, only a slight decrease of 5% in inhibitory activity is observed when Putranjiva roxburghii trypsin inhibitor is incubated for 2 h at 100 mM dithiothreitol 75359 3.4.21.4 Sagittaria sagittifolia arrowhead protease inhibitor A API-A 151548 3.4.21.4 small glossy black soybean trypsin inhibitor inhibitory activity is stable in the pH range 3-13 and in the temperature range 0-60°C, is inhibited by dithiothreitol (5-25 mM) in a dose-dependent manner 75360 3.4.21.4 sodium dodecylsulfate 0.5% w/v, no residual activity 1066 3.4.21.4 soybean Bowman-Birk inhibitor inhibition of HzTrypsin-C,no inhibition of HzTrypsin-S 117775 3.4.21.4 soybean Kunitz trypsin inhibitor strong inhibition of HzTrypsin-C, no inhibition of HzTrypsin-S 22533 3.4.21.4 soybean Kunitz trypsin inhibitor - 22533 3.4.21.4 soybean Kunitz trypsin inhibitor 80% of trypsin activity can be inhibited by 42 nM soybean Kunitz trypsin inhibitor 22533 3.4.21.4 Soybean trypsin inhibitor IC50: 0.000009 mM 544 3.4.21.4 Soybean trypsin inhibitor 0.1 mg/ml, isoenzyme aT-I loses 95% of its activity, isoenzyme aT-II loses 97% of its activity 544 3.4.21.4 Soybean trypsin inhibitor - 544 3.4.21.4 Soybean trypsin inhibitor complete inhibition 544 3.4.21.4 Soybean trypsin inhibitor 0.025% w/v, 0.3% residual activity 544 3.4.21.4 Soybean trypsin inhibitor strong 544 3.4.21.4 Soybean trypsin inhibitor effective inhibitor 544 3.4.21.4 Soybean trypsin inhibitor 91% inhibition at 1mg/ml 544 3.4.21.4 Soybean trypsin inhibitor 84.2% inhibition at 1 mg/ml 544 3.4.21.4 Soybean trypsin inhibitor isozyme TryIII activity is completely (more than 95%) inhibited by soybean trypsin inhibitor 544 3.4.21.4 Soybean trypsin inhibitor 96% inhibition at 1 mM 544 3.4.21.4 Soybean trypsin inhibitor complete inhibition at 1 mg/ml 544 3.4.21.4 Soybean trypsin inhibitor SBT, complete inhibition at 1 mg/ml 544 3.4.21.4 Soybean trypsin inhibitor 84% inhibition at 1 mg/ml 544 3.4.21.4 Soybean trypsin inhibitor 80% inhibition at 1 mg/ml 544 3.4.21.4 Soybean trypsin inhibitor 91.5% inhibition at 1 mg/ml 544 3.4.21.4 Soybean trypsin inhibitor different Kunitz trypsin inhibitors, KTIs, from different soybean lines, 15 soybean experimental lines and varieties, overview 544 3.4.21.4 Soybean trypsin inhibitor a Kunitz trypsin inhibitor from soybean seeds, identification of mutants, several polymorphic types that are controlled by multiple alleles, overview. Development of a single nucleotide amplified polymorphism marker for the classification of the predominant KTi types, Tia and Tib, and evaluation of KTi activities by differing KTi type total 451 soybean mutant lines, overview. Trypsin inhibitor type and trypsin inhibitor activity in TIU/mg, overview 544 3.4.21.4 Soybean trypsin inhibitor a serine protease inhibitor, complete inhibition of trypsin isozymes A, B and C at 1 mg/ml 544 3.4.21.4 Soybean trypsin inhibitor 1 mg/ml, 80% inhibition; 80.3% inhibition at 1 mg/ml 544 3.4.21.4 Soybean trypsin inhibitor 75.6% inhibition 544 3.4.21.4 Soybean trypsin inhibitor 250 mM, complete inhibition 544 3.4.21.4 Soybean trypsin inhibitor 0.01 mM, more than 95% inhibition 544 3.4.21.4 Spinacia oleracea trypsin inhibitor high affinity between trypsin and Spinacia oleracea trypsin inhibitor 75352 3.4.21.4 sun flower trypsin inhibitor-1 - 151552 3.4.21.4 sunflower trypsin inhibitor 1 SFTI-1, binding and effects on human prostate cancer cells, overview 159921 3.4.21.4 sunflower trypsin inhibitor-1 SFTI-1 14152 3.4.21.4 sunflower trypsin inhibitor-1 SFTI-1, a natural 14-residue cyclic peptide, can be used for enzyme separation from other serine proteases, synthesis of SFTI-1-based supports and affinity chromatography, overview. Inhibition of trypsin by some acyclic SFTI-1 analogues, e.g. [Lys5]-SFTI-1, [Arg5]-SFTI-1, and [Phe5]-SFTI-1, no inhibition by [Leu5]-SFTI-1, overview 14152 3.4.21.4 SVIGCWTKSIPPRPCFVK-amide HV-BBI is a Bowman-Birk type protease inhibitor from the skin secretion of the Chinese Bamboo odorous frog Huia versabilis, SVIGCWTKSIPPRPCFVK-amide is a synthetic replicate of HV-BBI with the wild-type K (Lys8) residue in the presumed P1 position and is a potent, competitive, and reversible inhibitor of trypsin 75350 3.4.21.4 SVIGCWTRSIPPRPCFVK-amide HV-BBI is a Bowman-Birk type protease inhibitor from the skin secretion of the Chinese Bamboo odorous frog Huia versabilis, SVIGCWTRSIPPRPCFVK-amide is a synthetic replicate of HV-BBI with the mutant R (Arg8) residue in the presumed P1 position and is a competitive, and reversible inhibitor of trypsin with reduced potency compared to the wild type peptide SVIGCWTKSIPPRPCFVK-amide 75351 3.4.21.4 T5E/N18R/T20G/P21S/T22D/K31M mutant Schistocerca gregaria protease (trypsin) inhibitor 1 the mutant inhibitor is improved compared to the wild-type inhibitor protein 167788 3.4.21.4 Tamarindus indica trypsin inhibitor a Kunitz-type inhibitor 159922 3.4.21.4 thionine from cowpea, inhibits trypsin, no inhibition of chymotrypsin 30918 3.4.21.4 tissue inhibitor of matrix metalloproteinases-2 TIMP-2, prevents the C-terminal truncation of activated metalloproteinase-2, without affecting the generation of the initial 62 kDa activated species 60783 3.4.21.4 tosyl-L-lysine-chloromethyl ketone - 139022 3.4.21.4 tosyl-L-lysyl chloromethyl ketone - 18963 3.4.21.4 tosyl-L-Phe chloromethyl ketone - 44883 3.4.21.4 TPI-1 - 151556 3.4.21.4 TPI-2 - 151557 3.4.21.4 trans-epoxysuccinyl-L-leucylamido-(4-guanidino) butane - 67562 3.4.21.4 trans-epoxysuccinyl-L-leucylamido-(4-guanidino)butane - 1306 3.4.21.4 trypsin inhibitor I-S Type from soybean reversible trypsin inhibitor 151563 3.4.21.4 trypsin modulating oostatic factor the hexapeptide NPTNLH is secreted at the last stage of vitellogenesis and inhibits the biosynthesis of trypsin in insect midgut cells 151550 3.4.21.4 tumor-associated trypsin inhibitor specific inhibition of degradation of gelatin and collagen type II 35827 3.4.21.4 tumor-associated trypsin inhibitor very efficient inhibition of trypsin-1 and trypsin-2, but not of trypsin-4 35827 3.4.21.4 tumor-associated trypsin inhibitor i.e. TATI, endogenous inhjibitor expressed in the cytoplasm of colon mucosa and colorectal cancer cells, shows prognostic significance of tumour-specific TATI expression in colorectal cancer, inhibitor expression is associated with a significantly decreased overall survival of colon cancer patients, and with increased liver metastasis, overview 35827 3.4.21.4 ulinastatin - 75355 3.4.21.4 urinary trypsin inhibitor urinary trypsin inhibitor reduces nuclear factor-kappa B activation and downregulates the expression of its related mediators, followed by the inhibition of neutrophil aggregation and infiltration in hepatic ischemiareperfusion injury 14670 3.4.21.4 urinary trypsin inhibitor - 14670 3.4.21.4 urinary trypsin inhibitor a Kunitz type protease inhibitor 14670 3.4.21.4 urinary trypsin inhibitor also known as bikunin 14670 3.4.21.4 urinary trypsin inhibitor also known as ulinastatin 14670 3.4.21.4 Vigna angularis trypsin inhibitor from adzuki beans, 13 kDa, isolated by heat treatment and ammonium sulfate fractionation 159919 3.4.21.4 Vigna mungo trypsin inhibitor purification of the Bowman-Birk proteinase inhibitor from the seeds of black gram, Vigna mungo cv. TAU-1. 8041.5 Da by mass spectrometry, pI 4.3-6.0, stable up to 80°C and at pH 2.0-12.0, analysis of the secondary structural conformation, overview, exhibts non-competitive-type inhibitory activity against both bovine pancreatic trypsin 80784 3.4.21.4 wild-type soybean inhibitor WBTI 151554 3.4.21.4 zeamatin - 117778 3.4.21.4 Zn2+ 18% inhibition at 5 mM 14 3.4.21.4 Zn2+ 71% inhibition at 5 mM 14 3.4.21.4 Zn2+ - 14 3.4.21.4 Zn2+ 10 mM, 31.6% inhibition 14 3.4.21.4 [4-(6-chloro-naphthalene-2-sulphonyl)piperazin-1-yl]-(3,4,5,6-tetrahydro-[2H-1,4']bipyridinyl-4-yl)-methanone - 22534 3.4.21.4 [Abu(3, 11)]-sun flower trypsin inhibitor-1 - 151551 3.4.21.4 [Arg5]-SFTI-1 a wild-type SFTI-1 analogue 80776 3.4.21.4 [Lys5]-SFTI-1 a wild-type SFTI-1 analogue 80775 3.4.21.4 [N,N'-bis(m-amidinosalicylidene)ethylenediaminato]copper(II) - 159915 3.4.21.4 [N,N'-bis(m-guanidinosalicylidene)ethylenediaminato]copper(II) - 159913 3.4.21.4 [Phe5]-SFTI-1 a wild-type SFTI-1 analogue 80777