Post-translational Modifications of Human Thrombin-Activatable Fibrinolysis Inhibitor (TAFI): Evidence for a Large Shift in the Isoelectric Point and Reduced Solubility upon Activation-Reference-Cited by-同舟云学术

Post-translational Modifications of Human Thrombin-Activatable Fibrinolysis Inhibitor (TAFI): Evidence for a Large Shift in the Isoelectric Point and Reduced Solubility upon Activation

Published:2006-01-12 Issue:5 Volume:45 Page:1525-1535
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Valnickova Zuzana¹,Christensen Trine¹,Skottrup Peter¹,Thøgersen Ida B.¹,Højrup Peter¹,Enghild Jan J.¹

Affiliation:

1. Center for Insoluble Protein Structure (inSPIN) at the Department of Molecular Biology, Science Park, University of Aarhus, Gustav Wied's Vej 10C, 8000 Aarhus C, Denmark, and Department of Biochemistry and Molecular Biology, University of Southern Denmark, Odense, Denmark

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi051956v

Reference45 articles.

1. A labile enzyme in fresh human serum interferes with the assay of carboxypeptidase N.

2. Isolation, molecular cloning, and partial characterization of a novel carboxypeptidase B from human plasma.

3. Plasma carboxypeptidases as regulators of the plasminogen system.

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