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Heterogeneity of Human Sphingomyelinase: Relatedness of the Major Polypeptides

  • John W. Callahan
  • Paula M. Strasberg
  • D. Joan Davidson
  • Prema Shankaran
  • Elizabeth Jobb
Part of the NATO ASI Series book series (NSSA, volume 116)

Abstract

Sphingomyelinase has been purified from the placenta, brain and urine (1–4). In most instances multiple polypeptides were seen. Jones et al (1) obtained a highly purified preparation from placenta which showed a major component at 89 kDa and minor ones at 70, 48 and 30 kDa, respectively. Sakuragawa found a major polypeptide for the placental enzyme at 70 kDa with a minor one at 40 kDa (2) while Yamanaka and Suzuki (3) obtained a single polypeptide at 70 kDa for the brain enzyme. Similarly Weitz et al (4) obtained bands at 73 and 28 kDa respectively for the enzyme from urine. All but the latter preparations were enriched at least 10,000-fold.

Keywords

Gauche Disease Marker Lane Acid Sphingomyelinase High Molecular Weight Component Major Polypeptide 
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 1986

Authors and Affiliations

  • John W. Callahan
    • 1
    • 2
  • Paula M. Strasberg
    • 1
    • 2
  • D. Joan Davidson
    • 1
    • 2
  • Prema Shankaran
    • 1
    • 2
  • Elizabeth Jobb
    • 1
    • 2
  1. 1.The Research InstituteThe Hospital for Sick ChildrenTorontoCanada
  2. 2.Departments of Pediatrics, Biochemistry Clinical BiochemistryUniversity of TorontoTorontoCanada

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