Abstract
The electrophoretic mobility of hexokinase from human erythrocytes and other tissues was studied with a new method that depends on the fluorescence of reduced nicotinamide-adenine dinucleotide phosphate for detecting enzyme activity on starch gel. The hexokinase of cord-blood erythrocytes has slightly different electrophoretic properties from that of adult red cells. Type I enzyme is split into type I(A) and type I(F); the latter is more intense in cord blood; in hemolyzates of adult blood, the activity of the two bands is usually about equal. No type II enzyme was found in cord blood. The double type I band was present in red cells from adult rabbits.
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