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Further studies of the turnover of dog antithrombin III. Study of /sup 131/I-labelled antithrombin protease complexes

Journal Article · · Thromb. Res.; (United States)
Fresh plasma containing /sup 131/I-antithrombin III (*I-AT) was coagulated and incubated at 37 degrees C for 2 hr. A ''complex peak,'' separated on heparin-agarose contained AT and *I-AT antigen but no heparin cofactor activity. Crossed immunoelectrophoresis showed only AT complexes. SDS PAGE showed 80% of the *I-AT in a major band (approximately 80,000 daltons), 15% in a minor band (approximately 100,000 daltons) and the rest in trace bands (approximately 60,000 and/or 115,000 daltons). Ammonia treatment of the complex peak released alpha-thrombin. After i.v. injection 80% of the complexed *I-AT, chiefly as the major band, left the plasma with t 1/2 approximately 15 min and was almost immediately catabolized to low molecular weight breakdown products. A major catabolic site was the liver. A simple kinetic model describes the findings approximately.
Research Organization:
Department of Medicine, University of Colorado Health Sciences Center, Denver
OSTI ID:
5394649
Journal Information:
Thromb. Res.; (United States), Journal Name: Thromb. Res.; (United States) Vol. 30:2; ISSN THBRA
Country of Publication:
United States
Language:
English