| Literature DB >> 11691627 |
M A Ibrahim1, A H Ghazy, T M Maharem, M I Khalil.
Abstract
An inhibitor of factor Xa (FXa) was isolated from the nymphs of the camel tick Hyalomma dromedarii by a combination of chromatography on DEAE-cellulose and Sephacryl S-300 columns. The isolated nymphal FXa inhibitor turned out to be a homogenous preparation of a single polypeptide chain (15 kDa) as judged by both the native and denatured SDS-PAGE. Its pI value ranged from 7.7 to 7.9. The inhibitor is a potent anticoagulant since it prolonged both the activated partial thromboplastin time (APTT) and the prothrombin time (PT) of the camel plasma in a concentration-dependent manner. Its activity was threefold lower toward thrombin than FXa, but it did not inhibit any of the proteases; trypsin, alpha-chymotrypsin, papain, pepsin and subtilisin. The inhibitor binds at two sites on FXa uncompetitively with an inhibition constant (K(i)) value of 134 nM.Entities:
Mesh:
Substances:
Year: 2001 PMID: 11691627 DOI: 10.1016/s1096-4959(01)00459-6
Source DB: PubMed Journal: Comp Biochem Physiol B Biochem Mol Biol ISSN: 1096-4959 Impact factor: 2.231