Hexosaminidases: Multiple Component Enzymes
In 1968 Robinson and Stirling (1) demonstrated that lysosomal N-acetylhexosaminidase could be separated into two species by starch gel electrophoresis. They noted that the more anodic form, A, was heat-labile and that it could be converted to the less anodic form, B, by the action of neuraminidase. In the intervening years, several groups have used various methods of purification of these two species and have compared the similarities and differences between them (2, 3,4). The two enzymes appear remarkably similar in amino acid composition, molecular weight, kinetic properties and, when highly purified have reported similar hydrolytic properties (4,5).
KeywordsDEAE Cellulose DEAE Cellulose Column Dixon Plot Cellulose Acetate Electrophoresis Ally Disorder
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