EC Number |
Application |
Reference |
---|
3.4.21.50 | analysis |
development of an achromopeptidase lysis procedure for high-volume testing and preparation of samples for PCR detection of methicillin-resistant Staphylococcus aureus. The BD GeneOhm MRSA kit method shows a sensitivity of 92.0%, specificity of 94.6%, positive predictive value of 75.4%, and negative predictive value of 98.5%. The assay is an accurate and rapid test for detection of MRSA colonization |
717910 |
3.4.21.50 | analysis |
endoproteinase lysine-C (Lys-C)/trypsin sequential digestion can be used in human 293T cell proteomics sample preparation, evaluation of the advantages of Lys-C/trypsin sequential digestion over trypsin digestion in solution conditions in different aspects, method optimzation, overview |
753287 |
3.4.21.50 | analysis |
method for identification of both the amino and the carboxyl termini of proteins. The method independently uses two proteases, Lys-C and peptidyl-Lys metalloendopeptidase Lys-N, to digest proteins, followed by LC-MS/MS analysis of the two digests. Terminal peptides can be identified as the amino terminal peptide of a protein in Lys-C digest is one lysine residue mass heavier than that in Lys-N digest, the carboxyl terminal peptide in Lys-N digest is one lysine residue mass heavier than that in Lys-C digest, and all internal peptides give exactly the same molecular masses in both the Lys-C and the Lys-N digest, although amino acid sequences of Lys-C and Lys-N peptides are different. Acetylation on N-terminus and protein isoforms, which have different termini, is also determined |
718383 |
3.4.21.50 | analysis |
middle-down approach, where the antibody is subjected to limited digestion using the endoproteinase Lys-C, is potentially useful for the accurate, sensitive and routine characterization of recombinant antibodies |
709430 |
3.4.21.50 | analysis |
the enzyme is attractive for the proteolytic generation of peptides to be analyzed by mass spectrometry, usage in quantitative mass spectrometry, overview. It can be used in the presence of protein denaturants which allow better access to cleavage sites and hence better proteolysis. The enzyme has advantages over trypsin, namely, reduced missed cleavage (because KR and RK are cleaved specifically), tolerance to denaturants and requirement for only a single labelled amino acid in experiments using isotopic labelling |
732899 |
3.4.21.50 | analysis |
the enzyme is used for rapid lysis of gram-positive cocci for pulsed-field gel electrophoresis |
36611 |
3.4.21.50 | analysis |
the enzyme is useful in the determination of primary structure of proteins |
36613 |
3.4.21.50 | biotechnology |
Lys C is used for protein digestion to yield at least two labeling sites with a mass difference of 4 Da. Dimethyl multiplex labelled peptides are analysed by MALDI-TOF. This technique enables investigating time course or dosage dependence of protein expressions. |
683404 |
3.4.21.50 | biotechnology |
Lys C is used to incorporate two 18O atoms into the carboxyl termini of peptides for proteomics |
683817 |
3.4.21.50 | medicine |
following infection with Pseudomonas aeruginosa, Ca2+ increase in the cornea can favor production of enzyme, which has been associated with corneal damage |
-, 670122 |