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Effect of Bacterial Neuraminidase on the Isoenzymes of Acid Hydrolases of Human Brain and Liver

  • J. A. Kint
  • A. Huys
Chapter
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 25)

Abstract

A number of lysosomal enzymes are known to occur in multiple forms. Physical and kinetic properties such as thermolability, pH-optimum or electrophoretic mobility are used in differentiating or separating such isoenzymes. As these hydrolases, which have a low specifity, are responsible for the degradation of large macromolecules such as glycolipids, mucopolysaccharides and glycoproteins, the question may arise on the physiological meaning of multiple forms. In this study more details on the occurrence and on the molecular differences of these isoenzymes in human brain and liver are presented.

Keywords

Sialic Acid Acid Phosphatase Lysosomal Enzyme Acid Fraction Clostridium Perfringens 
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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References

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Copyright information

© Plenum Press, New York 1972

Authors and Affiliations

  • J. A. Kint
    • 1
  • A. Huys
    • 1
  1. 1.Department of PediatricsAkademisch ZiekenhuisGhentBelgium

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