Abstract
Quantitative differences in the enzyme activities of fetal and adult red cells are well known, but few data on differences in the isoenzyme patterns between these cells have been published. In this study isoenzymes of phosphopyruvatee hydratase (EC.4.2.1.11) and pyruvate kinase (EC.2.7.1.40) were investigated in hemolysates of isolated fetal and adult erythrocytes. Electrophoresis was performed on cellulose acctate foils. Sites of enzyme activity were detected utilizing the fluorescence of nicotinamide adenine dinucleotide by illuminating the foils with ultraviolet light after incubation with specific identification-reaction mixtures. For both phosphopyruvate hydratase and pyruvate kinase differences in number, intensity, and/or clectrophorectic mobility of isoenzyme bands between fetal and adult erythrocytes could be demonstrated. These findings suggest further evidence for the biochemical distinction of fetal and adult red cells.
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