The Effects of Nonenzymatic Glycation on Human α2-Plasmin Inhibitor in Vitro

The Effects of Nonenzymatic Glycation on Human α2-Plasmin Inhibitor in Vitro

We studied the effects of nonenzymatic glycation on human α2-plasmin inhibitor (α2-PI) in vitro. Purified human α2-PI (14.9μM/l) was incubated with glucose (55.5mM/l) at 37°C for 4 days. α2-PI was significantly glycated, and then the activity of glycated α2-PI decreased, while the levels of α2-PI an...

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Veröffentlicht in:Japanese Journal of Thrombosis and Hemostasis 1994/06/01, Vol.5(3), pp.182-189
Hauptverfasser: YAMASHITA, Tsutomu, FUJII, Seiji, INOUE, Kaori, HATAKEDA, Noriko, KOBAYASHI, Emi, MATSUOKA, Akira
Format: Artikel
Sprache:eng
Schlagworte:
active site binding site (ABS)
kringle binding site (KBS)
lysine binding site I (LBS I)
nonenzymatic glycation
α2-Plasmin inhibitor
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Zusammenfassung:We studied the effects of nonenzymatic glycation on human α2-plasmin inhibitor (α2-PI) in vitro. Purified human α2-PI (14.9μM/l) was incubated with glucose (55.5mM/l) at 37°C for 4 days. α2-PI was significantly glycated, and then the activity of glycated α2-PI decreased, while the levels of α2-PI antigen did not change. The amount of complexes which were formed between glycated α2-PI and plasmin (5.0U/ml) were less than that of control (control: 167.0-354.8nM/l, glycated α2-PI: 25.2-105.4nM/l, p
ISSN:0915-7441
1880-8808
DOI:10.2491/jjsth.5.182