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Literature summary for 1.7.6.1 extracted from

  • Andersen, J.F.; Gudderra, N.P.; Francischetti, I.M.; Valenzuela, J.G.; Ribeiro, J.M.
    Recognition of anionic phospholipid membranes by an antihemostatic protein from a blood-feeding insect (2004), Biochemistry, 43, 6987-6994.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Rhodnius prolixus

Protein Variants

Protein Variants Comment Organism
K149A using 3:1 phosphatidylcholine:phosphatidylserine vesicles, binding is reduced by a factor of three from that observed with wild-type protein, suggesting that this region does play an important role in phospholipid binding Rhodnius prolixus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
20600
-
x * 20600, calculated from sequence Rhodnius prolixus

Organism

Organism UniProt Comment Textmining
Rhodnius prolixus Q6PQK2
-
-

Purification (Commentary)

Purification (Comment) Organism
the NP7 protein is obtained as inclusion bodies and is denatured, refolded, and reconstituted with heme as described for other nitrophorins. The refolded reconstituted protein is purified by a two-step procedure Rhodnius prolixus

Source Tissue

Source Tissue Comment Organism Textmining
saliva the salivary protein binds with high affinity to anionic phospholipid membranes. The protein is apparently targeted to the negatively charged surfaces of activated platelets and other cells where it can serve as a vasodilator, antihistamine, platelet aggregation inhibitor, and anticoagulant Rhodnius prolixus
-

Subunits

Subunits Comment Organism
? x * 20600, calculated from sequence Rhodnius prolixus

Synonyms

Synonyms Comment Organism
Nitrophorin 7
-
Rhodnius prolixus
NP7
-
Rhodnius prolixus

pH Stability

pH Stability pH Stability Maximum Comment Organism
4 5 the enzyme-NO complex is more stable at pH 4-5 than at physiologic pH. pH. In pH 4.5 sodium acetate buffer, a complex formed by incubation with S-nitroso-N-acetylpenicillamine is stable for several hours at room temperature, is purified by gel filtration chromatography at pH 4.5, and maintains indefinitely at -20°C. Raising the pH of the complex solution by adding concentrated Tris-HCl, pH 7.5 results in dissociation of the complex over a period of 10-15 min Rhodnius prolixus
7.5
-
the enzyme-NO complex is more stable at pH 4-5 than at physiologic pH. pH. In pH 4.5 sodium acetate buffer, a complex formed by incubation with S-nitroso-N-acetylpenicillamine is stable for several hours at room temperature, is purified by gel filtration chromatography at pH 4.5, and maintains indefinitely at -20°C. Raising the pH of the complex solution by adding concentrated Tris-HCl, pH 7.5 results in dissociation of the complex over a period of 10-15 min Rhodnius prolixus

pI Value

Organism Comment pI Value Maximum pI Value
Rhodnius prolixus calculated from sequence
-
8.72

General Information

General Information Comment Organism
physiological function NP7 inhibits prothrombin activation by blocking phospholipid binding sites for the prothrombinase complex on the surfaces of vesicles and activated platelets. As a NO complex, NP7 inhibits collagen and ADP-induced platelet aggregation and induces disaggregation of ADP-stimulated platelets by an NO-mediated mechanism Rhodnius prolixus