Understanding the fluorescence changes of human plasminogen when it binds the ligand, 6-aminohexanoate: a synthesis.
This work attempts to explain several aspects of the response of plasminogen to 6-aminohexanoate (6-AH). These responses include the overall fluorescent changes that occur when plasminogen binds the ligand, the changes shown by the individual domains when they bind the ligand, and the changes in structure shown by the holoprotein when it binds 6-AH. The results have implications for understanding the physicochemical behavior of all kringle based proteins.
Kornblatt
J A
JA
Enzyme Research Group, Concordia University, 1455 de Maisonneuve Ouest, Montreal, Quebec, Canada. krnbltt@vax2.concordia.ca
D015119:Aminocaproic Acid / Q000737:chemistry*; D000933:Antifibrinolytic Agents / Q000737:chemistry*; D005453:Fluorescence; D006801:Humans; D018082:Kringles; D008024:Ligands; D010958:Plasminogen / Q000037:antagonists & inhibitors / Q000737:chemistry*; D014364:Tryptophan / Q000737:chemistry
D000933:Antifibrinolytic Agents; D008024:Ligands; D014364:Tryptophan; D010958:Plasminogen; D015119:Aminocaproic Acid