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Hexosaminidases: Multiple Component Enzymes

  • J. A. Lowden
  • J. W. Callahan
  • F. N. Howard
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 68)

Abstract

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).

Keywords

DEAE Cellulose DEAE Cellulose Column Dixon Plot Cellulose Acetate Electrophoresis Ally Disorder 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Plenum Press, New York 1976

Authors and Affiliations

  • J. A. Lowden
    • 1
  • J. W. Callahan
    • 1
  • F. N. Howard
    • 1
  1. 1.Research InstituteThe Hospital for Sick ChildrenTorontoCanada

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