Structural evidence for leucine at the reactive site of heparin cofactor II
- 19 November 1985
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 24 (24), 6777-6782
- https://doi.org/10.1021/bi00345a008
Abstract
Note: In lieu of an abstract, this is the article's first page.This publication has 21 references indexed in Scilit:
- Identification of the cleavage sites resulting from enzymic inactivation of human antithrombin III by Crotalus adamanteus proteinase II in the presence and absence of heparinBiochemistry, 1981
- Dissociation of antithrombin III-thrombin complex. Formation of active and inactive antithrombin IIIBiochemistry, 1981
- Enzymatic in activation of human antithrombin III limited proteolysis of the inhibitor by snake venom proteinases in the presence of heparinBiochimica et Biophysica Acta (BBA) - Enzymology, 1980
- Kinetics of association of serine proteinases with native and oxidized alpha-1-proteinase inhibitor and alpha-1-antichymotrypsin.Journal of Biological Chemistry, 1980
- Structural evidence for methionine at the reactive site of human alpha-1-proteinase inhibitor.Journal of Biological Chemistry, 1978
- Automated amino acid sequence of small peptides utilizing PolybreneAnalytical Biochemistry, 1978
- Polyquarternary amines prevent peptide loss from sequenatorsAnalytical Biochemistry, 1978
- Thrombin adsorption to surfaces and prevention with polyethylene glycol 6,000Thrombosis Research, 1976
- Highly Purified Antithrombin III with Heparin Cofactor Activity Prepared by Disc ElectrophoresisScandinavian Journal of Clinical and Laboratory Investigation, 1968
- A Protein SequenatorEuropean Journal of Biochemistry, 1967