Properties of chemically modified protein S: the effect of the conversion of .gamma.-carboxyglutamic acid to .gamma.-methyleneglutamic acid on functional properties-Reference-Cited by-同舟云学术

Properties of chemically modified protein S: the effect of the conversion of .gamma.-carboxyglutamic acid to .gamma.-methyleneglutamic acid on functional properties

Published:1986-10-07 Issue:20 Volume:25 Page:6305-6311
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Walker Frederick J.

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi00368a071

Reference48 articles.

1. Decarboxylation of gamma-carboxyglutamic acid residues in human prothrombin. Stoichiometry of calcium binding to gamma-carboxyglutamic acid in prothrombin.

2. Molecular weight of human high-molecular-weight kininogen light chain by equilibrium sedimentation in an air-driven ultracentrifuge

3. Recurrent Venous Thromboembolism in Patients with a Partial Deficiency of Protein S

4. Characterization of protein S, a .gamma.-carboxyglutamic acid containing protein from bovine and human plasma

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3. Human protein S inhibits prothrombinase complex activity on endothelial cells and platelets via direct interactions with factors Va and Xa.;Journal of Biological Chemistry;1994-08

4. Binding of protein S to C4b-binding protein. Mutagenesis of protein S.;Journal of Biological Chemistry;1992-04

5. Modifications of bovine prothrombin fragment 1 in the presence and absence of Ca(II) ions. Loss of positive cooperativity in Ca(II) ion binding for the modified proteins.;Journal of Biological Chemistry;1992-03