Degradation of Glu- and Lys-plasminogen by elastase in the presence or absence of tranexamic acid.
Glu-plasminogen (Glu-plg) was degraded by elastase in the presence or absence of tranexamic acid. Glu-plg was degraded faster in the presence of tranexamic acid. Increase in the concentration of tranexamic acid resulted in increase in the appearance of degradation products, reaching a plateau level at 1 mM of tranexamic acid. Fifty percent increase in the concentration of one of degradation products was obtained at 0.22 mM of tranexamic acid, which is similar to a dissociation constant (Kd) of low affinity lysine binding sites (LBS) with tranexamic acid. As to the degradation rate of two isozymes of Glu-plg (Glu-plg I and II), Glu-plg II containing one carbohydrate chain was degraded faster than Glu-plg I containing two carbohydrate chains. Comparison of the degradation rates of Glu-plg and Lys-plg indicated that Lys-plg was degraded faster.
Takada
A
A
Department of Physiology, Hamamatsu University, School of Medicine, Shizuoka-ken, Japan.
Sugawara
Y
Y
Takada
Y
Y
D003509:Cyclohexanecarboxylic Acids / Q000494:pharmacology*; D004305:Dose-Response Relationship, Drug; D007700:Kinetics; D010196:Pancreatic Elastase / Q000378:metabolism*; D010446:Peptide Fragments / Q000032:analysis / Q000378:metabolism*; D010958:Plasminogen / Q000378:metabolism*; D011487:Protein Conformation; D014148:Tranexamic Acid / Q000494:pharmacology*
D003509:Cyclohexanecarboxylic Acids; D010446:Peptide Fragments; C018998:lysyl-plasminogen; D014148:Tranexamic Acid; D010958:Plasminogen; D010196:Pancreatic Elastase