Analysis of ligand binding to kringles 4 and 5 fragments from human plasminogen.
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.
Novokhatny
V V
VV
Institute of Biochemistry, Academy of Sciences of the Ukrainian, Kiev, USSR.
Matsuka YuV
Kudinov
S A
SA
D000588:Amines / Q000378:metabolism; D015119:Aminocaproic Acid / Q000378:metabolism; D001120:Arginine / Q000378:metabolism; D001665:Binding Sites; D006801:Humans; D066298:In Vitro Techniques; D007700:Kinetics; D008239:Lysine / Q000378:metabolism; D010421:Pentanoic Acids / Q000378:metabolism; D010958:Plasminogen / Q000378:metabolism*; D013816:Thermodynamics
D000588:Amines; D010421:Pentanoic Acids; D010958:Plasminogen; D001120:Arginine; C005264:n-amylamine; D008239:Lysine; D015119:Aminocaproic Acid