Purification, electrophoretic characterization and plasma concentrations of feline or canine antithrombin III.
- 1 January 1985
- journal article
- research article
- Published by Japanese Society of Veterinary Science in The Japanese Journal of Veterinary Science
- Vol. 47 (6) , 987-994
- https://doi.org/10.1292/jvms1939.47.987
Abstract
Feline or canine antithrombin III (AT III) was purified from plasma by salt precipitations and heparin-attached Sepharose CL-6B. For the isolation of canine AT III, an additional ion exchange chromatography was needed for the final purification. The two purified proteins showed similar characteristics with cellulose acetate, agarose, polyacrylamide gel or immunoelectrophoresis, having the molecular weight of approximately 62,000. The isoelectric points were 4.70 and 4.75 for feline: 4.70, 4.75 and 4.80 for canine AT III. Thrombin inhibition activity of the purified proteins was reinforced in the presence of heparin. Anti-feline and anti-canine AT III sera formed precipitin lines against feline and canine plasma, but not against human, Japanese monkey, rat or mouse plasma. Concentrations of AT III and levels of heparin cofactor activity in plasma were measured by Laurell''s electroimmunoassay and enzymatic assay technics, respectively. Values for feline plasma were: 0.50 .+-. 0.1 (mean .+-. standard deviation) g/l; 198.57 .+-. 33.1 NIH U/ml; and for canine plasma: 0.49 .+-. 0.1 g/l; 178.51 .+-. 26.0 NIH U/ml.This publication has 1 reference indexed in Scilit:
- Quantitative estimation of proteins by electrophoresis in agarose gel containing antibodiesAnalytical Biochemistry, 1966