Hexokinase isoenzymes in human erythrocytes.
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.
D000818:Animals; D004586:Electrophoresis; D004912:Erythrocytes / Q000201:enzymology*; D005453:Fluorescence; D006461:Hemolysis; D006593:Hexokinase / Q000097:blood*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007527:Isoenzymes / Q000097:blood*; D009249:NADP; D011817:Rabbits; D013213:Starch; D014470:Umbilical Cord / Q000098:blood supply
D007527:Isoenzymes; D009249:NADP; D013213:Starch; D006593:Hexokinase