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Merck
  • Analysis of ligand binding to kringles 4 and 5 fragments from human plasminogen.

Analysis of ligand binding to kringles 4 and 5 fragments from human plasminogen.

Thrombosis research (1989-02-01)
V V Novokhatny, Matsuka YuV, S A Kudinov
摘要

The interaction of the isolated kringles 4 and 5 from human plasminogen with 6-aminohexanoic acid, pentylamine, pentanoic acid and arginine has been quantitatively characterized by scanning calorimetry and fluorescent spectroscopy. It has been found that the ligands with the positively charged group have a good binding ability while pentanoic acid in comparison with 6-aminohexanoic acid being devoid of amino group does not interact with the kringles under study. The positively charged group of the ligand is suggested to play a crucial role in ligand binding with the lysine-binding site.

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Sigma-Aldrich
戊胺, 99%
Sigma-Aldrich
戊胺, ≥99%, FG