Structure of the omega-aminocarboxylic acid-binding sites of human plasminogen. Arginine 70 and aspartic acid 56 are essential for binding of ligand by kringle 4.-Reference-Cited by-同舟云学术

Structure of the omega-aminocarboxylic acid-binding sites of human plasminogen. Arginine 70 and aspartic acid 56 are essential for binding of ligand by kringle 4.

Published:1982-07 Issue:13 Volume:257 Page:7401-7406
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Trexler M,Váli Z,Patthy L

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference30 articles.

1. The specific interaction between plasminogen and fibrin. A physiological role of the lysine binding site in plasminogen

2. On the specific interaction between the lysine-binding sites in plasmin and complementary sites in α2-antiplasmin and in fibrinogen

3. Molecular mechanism of physiological fibrinolysis

4. Quantitative determination of the binding of epsilon-aminocaproic acid to native plasminogen.

5. The binding of tranexamic acid to native (Glu) and modified (Lys) human plasminogen and its effect on conformation.

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