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The determination of a calcium-dependent binding constant of the bovine prothrombin Gla domain (residues 1-45) to phospholipid vesicles.

作者信息

Weber D J, Pollock J S, Pedersen L G, Hiskey R G

机构信息

Department of Chemistry, University of North Carolina, Chapel Hill 27599-3290.

出版信息

Biochem Biophys Res Commun. 1988 Aug 30;155(1):230-5. doi: 10.1016/s0006-291x(88)81073-8.

DOI:10.1016/s0006-291x(88)81073-8
PMID:3415682
Abstract

Calcium-mediated binding of the radioiodinated peptide representing residues 1-45 of bovine prothrombin to single bilayer phospholipid vesicles composed of phosphatidylserine from bovine brain and synthetic 1-palmitoyl-2-oleoyl-phosphatidylcholine (25:75 PS/PC) has been studied over peptide concentrations from 0.33 microM to 3.75 microM and at a calcium concentration of 1.0 mM. The binding isotherm for the interaction between the radioiodinated peptide and PS/PC vesicles fits a model in which there is noncooperative binding of the peptide to non-interacting sites on the phospholipid bilayer. A dissociation constant determined at these conditions is 11.8 microM compared to 1.0 microM for prothrombin fragment 1.

摘要

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