Novokhatny V V, Kudinov S A
Institute of Biochemistry, Academy of Sciences of the Ukrainian, Kiev, USSR.
Thromb Res. 1989 Feb 1;53(3):243-52. doi: 10.1016/0049-3848(89)90099-6.
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.
