On the occurrence of thrombin-like enzymes in mosquitoes

A thrombin-like enzyme has been identified in mosquitoes and partially purified. The enzyme preparation displays on SDS gel electrophoresis a major protein band of about 22 kDa and one minor of about 28 kDa. The enzyme preparation cleaves a synthetic substrate (S-2238) for thrombin with Km 113 μmol/...

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Bibliographic Details
Published in:Thrombosis research 1996-03, Vol.81 (6), p.623-634
Main Authors: Bark, Niklas, Blombäck, Birger, Fatah, Kamaran
Format: Article
Language:English
Subjects:
Aedes - enzymology
Aedes communis
Ammonium Sulfate
Animals
Biochemistry. Physiology. Immunology
Biological and medical sciences
Chemical Fractionation
Chromatography, Gel
clotting
enzyme
Ethanol
Fibrinolysis
Fundamental and applied biological sciences. Psychology
Insecta
Invertebrates
Medicin och hälsovetenskap
Molecular Weight
mosquito
Nephelometry and Turbidimetry
Physiology. Development
thrombin
Thrombin - isolation & purification
thrombin-like
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Summary:A thrombin-like enzyme has been identified in mosquitoes and partially purified. The enzyme preparation displays on SDS gel electrophoresis a major protein band of about 22 kDa and one minor of about 28 kDa. The enzyme preparation cleaves a synthetic substrate (S-2238) for thrombin with Km 113 μmol/L (as compared to 3 μmol/L for thrombin). The enzyme clots fibrinogen and plasma. During activation of fibrinogen, fibrinopeptide A (but scarcely fibrinopeptide B) is released. The enzyme is not inhibited by hirudin and activates (if at all) factor XIII differently from thrombin. Predominantly γ-dimers are formed in the cross linking process. As compared to thrombin a larger extent of activation is required to induce gelation (clotting) by the mosquito enzyme. At a given clotting time the enzyme produces tighter gel structures than thrombin. In its action the enzyme resembles the snake venom enzyme, batroxobin.
ISSN:0049-3848
1879-2472
DOI:10.1016/0049-3848(96)00038-2