Non-enzymatic glucosylation of fibrinogen.
Glucose, when incubated with fibrinogen, binds covalently to that protein. The reaction is non-enzymatic in type and is directly dependant on the time of incubation, temperature and pH. Glucosylation of fibrinogen is not altered by preincubation with aspirin. No preferential glucosylation of fibrinogen, fibrinogen chains or plasmin digestion products XYDE could be demonstrated, suggesting that glucose binding occur at several different sites. No abnormality of thrombin clotting or stability of glucosylated fibrinogen could be detected. These findings are discussed in relation to the previously described abnormalities of fibrinogen metabolism in diabetes mellitus.
D000418:Albumins / Q000378:metabolism; D001665:Binding Sites; D002852:Chromatography, Ion Exchange; D003920:Diabetes Mellitus / Q000201:enzymology*; D005340:Fibrinogen / Q000378:metabolism*; D005947:Glucose / Q000378:metabolism*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D013918:Thrombin Time; D014508:Urea / Q000494:pharmacology
D000418:Albumins; D014508:Urea; D005340:Fibrinogen; D005947:Glucose