Zinc binding by fibrin facilitates proteolysis by a snake (puffadder) venom protease
| Autor: | Dhesigen P. Naidoo, Langley R. Purves |
|---|---|
| Rok vydání: | 1992 |
| Předmět: |
Proteolysis
medicine.medical_treatment Molecular Sequence Data chemistry.chemical_element Peptide Zinc Plasma protein binding Viper Venoms Fibrin Fibrin Fibrinogen Degradation Products Endopeptidases medicine Amino Acid Sequence Peptide sequence chemistry.chemical_classification Protease medicine.diagnostic_test biology Hematology Enzyme chemistry Biochemistry biology.protein Cardiology and Cardiovascular Medicine Protein Binding |
| Zdroj: | Seminars in thrombosis and hemostasis. 18(2) |
| ISSN: | 0094-6176 |
| Popis: | PAV protease is able to cleave between the crosslinked sites of the gamma-chain of fibrin and fibrin-derived D-dimer. The rate of digestion can be increased fourfold to tenfold by the addition of zinc ions. Although the PAV protease is a zinc-containing metalloenzyme, the enhanced rate of cleavage can be shown to be due to histidine-specific zinc binding by D-dimer. It is proposed that zinc ions cause a distortion of the inter-crosslink peptide chain, creating a novel protease-susceptible site. The physiologic relevance is uncertain due to the relatively low measured zinc binding constant Kd = 10(-3.88) M. Zinc binding could, nevertheless, create a useful fibrin-specific neoepitope for antibody recognition in vitro. |
| Databáze: | OpenAIRE |
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