Effects of temperature, pH, and inhibitors on the procoagulant characterization of FIa, a factor X activator from the venom of Daboia russellii siamensis (Myanmar)
FIa, a factor X activator, was isolated from the venom of Daboia russellii siamensis (Myanmar) after a series of chromatographic separations. FIa displayed procoagulant activity by shortening plasma recalcification time and converted human factor X (FX) to activated human factor X (FXa) by cleaving...
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Published in | Archives of pharmacal research Vol. 33; no. 7; pp. 1043 - 1048 |
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Main Authors | , , , , , |
Format | Journal Article |
Language | English |
Published |
Heidelberg
Pharmaceutical Society of Korea
01.07.2010
대한약학회 |
Subjects | |
Online Access | Get full text |
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Summary: | FIa, a factor X activator, was isolated from the venom of
Daboia russellii siamensis
(Myanmar) after a series of chromatographic separations. FIa displayed procoagulant activity by shortening plasma recalcification time and converted human factor X (FX) to activated human factor X (FXa) by cleaving the heavy FX chain, possibly at the Arg51-Ile52 peptide. FIa was positive in a glycoprotein staining test, demonstrating that it is a glycoprotein. Optimal temperature and pH values were important for FIa procoagulant activity. Procoagulant activity was maintained above 85% of the initial activity at pH 7.0∼8.0, and showed equally maximum activity at temperatures ranging from 30 to 50°C. In addition, FIa procoagulant activity was completely inhibited by EDTA (5 mM), but not by PMSF (10 mM), suggesting that it is a metalloproteinase. |
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Bibliography: | ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 G704-000010.2010.33.7.006 |
ISSN: | 0253-6269 1976-3786 |
DOI: | 10.1007/s12272-010-0710-7 |