Active-site-selective labeling of blood coagulation proteinases with fluorescence probes by the use of thioester peptide chloromethyl ketones. II. Properties of thrombin derivatives as reporters of prothrombin fragment 2 binding and specificity of the labeling approach for other proteinases.-Reference-Cited by-同舟云学术

Active-site-selective labeling of blood coagulation proteinases with fluorescence probes by the use of thioester peptide chloromethyl ketones. II. Properties of thrombin derivatives as reporters of prothrombin fragment 2 binding and specificity of the labeling approach for other proteinases.

Published:1992-07 Issue:21 Volume:267 Page:14974-14981
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Bock P.E.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference33 articles.

1. Active site selective labeling of serine proteases with spectroscopic probes using thioester peptide chloromethyl ketones: demonstration of thrombin labeling using N.alpha.[(acetylthio)acetyl]-D-Phe-Pro-Arg-Ch2Cl

2. Active-site-selective labeling of blood coagulation proteinases with fluorescence probes by the use of thioester peptide chloromethyl ketones. I. Specificity of thrombin labeling.

3. Characteristics of the association between prothrombin fragment 2 and α-thrombin

4. The effect of bovine thrombomodulin on the specificity of bovine thrombin.

5. The effect of prothrombin fragment 2 on the inhibition of thrombin by antithrombin III.

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