Mechanism of the calcium-dependent self-association of bovine prothrombin. Use of a covalent cross-linking reagent to study the reaction.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference27 articles.
1. Multiple modes of association in bovine prothrombin and its proteolysis products.
2. Differentiation of metal ion-induced transitions of prothrombin fragment 1.
3. Self-association of bovine prothrombin fragment 1 in the presence of metal ions. Use of a covalent cross-linking reagent to study the reaction.
4. Influence of metal ions on prothrombin self-association. Demonstration of dimer formation by intermolecular cross-linking with dithiobis(succinimidylpropionate).
5. Metal ion interactions with bovine prothrombin and prothrombin fragment. 1. Stoichiometry of binding, protein self-association, and conformational change induced by a variety of metal ions
Cited by 7 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献
1. Comparison of the membrane binding kinetics of bovine prothrombin and its fragment 1.;Journal of Biological Chemistry;1993-11
2. Bifunctional Reagents for Bioorganic Syntheses. Bis-Enamines. Cross-Linking by Amine Exchange Reactions;Synthetic Communications;1990-09
3. A versatile, highly reactive, cross-linking reagent: 2,2′-Sulfonylbis[3-methoxy-(E,E)-2-propenenitrile];Biochemical and Biophysical Research Communications;1990-01
4. Amino-terminal alanine functions in a calcium-specific process essential for membrane binding by prothrombin fragment 1;Biochemistry;1988-06-28
5. Reversibility of prothrombin adsorption on lipid monolayers;Journal of Colloid and Interface Science;1988-05
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