Abstract
Human creatine kinase (CK) was demonstrated to be partly present as a glycated molecule. Sialic acid, galactose and sulfate were also found to be present on the molecule. The glycated forms were characterized by higher activation energies and were thermally unstable. Skeletal muscle CK showed lower relative binding towards the lectin concanavalin A (Con A) in comparison with the heart tissue forms. After skeletal muscle trauma, CK in serum was found to be less glycated than in tissue. After acute myocardial infarction (AMI), no glycated CK could be detected in serum. Following injury, it appears that the transfer from tissue to plasma is accompanied by a loss of glycated isoforms. High-voltage electrophoresis showed no differences in the distribution of CK isoforms between the glycated and non-glycated forms.
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