Kringle domains and plasmin denaturation.
The rate of plasmin denaturation was in the order of Lys-plasmin greater than miniplasmin greater than microplasmin. Fibrinogen degradation products (FDP) dose dependently increased the denaturation rate of Lys-plasmin and mini-plasmin with a maximal rate constant at the FDP/plasmin ratio of about 0.5. The denaturation rate constant of microplasmin was not affected. FDP increased the rate of plasmin denaturation was in parallel with its effect on the interaction among kringle domains. Without FDP only trace amounts of plasminogen dimer could be detected by cross-linking with bis-(sulfo-succinimidyl)-suberate followed by SDS gel electrophoresis. In the low concentration of FDP significant amounts of oligomers of Glu-, mini-plasminogens, kringle 1-3 and kringle 1-5 were observed. High concentration of FDP, however, decreased plasminogen oligomer.
Shi
G Y
GY
Biochemistry Department, Medical College, National Cheng-Kung University, Tainan, Taiwan, Republic of China.
Wu
D H
DH
Wu
H L
HL
D000595:Amino Acid Sequence; D003432:Cross-Linking Reagents; D005341:Fibrinolysin / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D007700:Kinetics; D008954:Models, Biological; D008970:Molecular Weight; D010958:Plasminogen / Q000302:isolation & purification / Q000378:metabolism; D011487:Protein Conformation; D011489:Protein Denaturation; D013388:Succinimides
D003432:Cross-Linking Reagents; D013388:Succinimides; D010958:Plasminogen; C035760:bis(sulfosuccinimidyl)suberate; D005341:Fibrinolysin