dc.contributor.author | Limo, M K | |
dc.contributor.author | Voigt, W P | |
dc.contributor.author | Tumbo-Oeri, A G | |
dc.contributor.author | Njogu, R M | |
dc.contributor.author | ole-MoiYoi, O K | |
dc.date.accessioned | 2013-06-10T07:01:17Z | |
dc.date.available | 2013-06-10T07:01:17Z | |
dc.date.issued | 1991 | |
dc.identifier.citation | Exp Parasitol. 1991 May;72(4):418-29 | en |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/pubmed/2026216 | |
dc.identifier.uri | http://erepository.uonbi.ac.ke:8080/xmlui/handle/123456789/30397 | |
dc.description.abstract | An anticoagulant isolated from salivary gland extracts of the ixodid tick Rhipicephalus appendiculatus was purified by gel filtration on Sephadex G-100, ion exchange on DEAE-cellulose, aprotinin-Sepharose, and by high-pressure-liquid size-exclusion chromatography. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis showed that the anticoagulant activity was associated with a protein of an apparent Mr of 65 kDa. The purified molecule had a pI in the range of 8.0-8.5 on chromatofocusing and was stable over a wide pH range, but was heat labile and susceptible to inactivation by trypsin and reductive alkylation. The anticoagulant did not inhibit thrombin-initiated fibrin formation and had no detectable fibrino(geno)lytic or phospholipase-like activities. Although it inhibited factor Xa-induced clotting of bovine plasma, it did not affect the amidase activity of factor Xa toward a synthetic substrate, suggesting that the anticoagulant acts at a site distinct from the active site of factor Xa or on other components of the prothrombinase complex | en |
dc.language.iso | en | en |
dc.title | Purification and characterization of an anticoagulant from the salivary glands of the ixodid tick Rhipicephalus appendiculatus | en |
dc.type | Article | en |
local.publisher | Department of Veterinary Microbiology and Immunology, University of California | en |
local.publisher | Department of Biochemistry, University of Nairobi | en |