Evidence for self-association of prothrombin fragment 1 in the absence of calcium ions. Implications for the interpretation of cooperativity of calcium binding.-Reference-Cited by-同舟云学术

Evidence for self-association of prothrombin fragment 1 in the absence of calcium ions. Implications for the interpretation of cooperativity of calcium binding.

Published:1987-10 Issue:28 Volume:262 Page:13472-13475
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Jackson C M,Brenckle G M,Hogg P J,Winzor D J

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference34 articles.

1. On the nature of allosteric transitions: A plausible model

2. Comparison of Experimental Binding Data and Theoretical Models in Proteins Containing Subunits*

3. A Theoretical Study of the Binding of Small Molecules to a Polymerizing Protein System. A Model for Allosteric Effects*

4. Vitamin K Metabolism and Vitamin K-dependent Proteins;Jackson,1980

5. Metal Ions in Biological Systems;Nelsestuen,1984

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1. Evidence for multiple enzyme site involvement in the modulation of thrombin activity by products of prothrombin proteolysis;Biophysical Chemistry;1998-12

2. Intramolecular domain-domain interactions and intermolecular self-association in bovine prothrombin. A potentiometric and laser light-scattering study;Journal of Protein Chemistry;1995-10

3. Comparison of the membrane binding kinetics of bovine prothrombin and its fragment 1.;Journal of Biological Chemistry;1993-11

4. Preferential ligand binding to multi-state acceptor systems: Comparisons of the calcium-binding and dimerization characteristics of prothrombin and fragment 1;Journal of Theoretical Biology;1991-12

5. Phospholipid binding properties of bovine prothrombin peptide residues 1-45.;Journal of Biological Chemistry;1988-10