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Phospholipase activity of rat tissues and its modification by trypsin1,2

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Lipids

Abstract

Treatment with proteolytic enzymes before the addition of the phospholipid substrate increases the activity of the phospholipases of the spleen, thymys, bone marrow, lung, and liver of the rat. In contrast, the phospholipase activity of the intestine, which is higher than that of all other normal tissues, is not increased when incubated with proteases. The results of fractionation studies by high-speed centrifugation and gel filtration and differences in enzyme kinetics support the conclusion that the intestinal phospholipases differ substantially from phospholipases found in the other tissues.

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Authors and Affiliations

  1. Department of Physiology and Pharmacology, Duke University Medical Center, Burham, North Carolina

    Athos Ottolenghi

Authors
  1. Athos Ottolenghi
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Additional information

Supported in part by Grant No. CA04605-06, US Public Health Service; Contract No. AT-(40-1)-3329, US Atomic Energy Commission.

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Ottolenghi, A. Phospholipase activity of rat tissues and its modification by trypsin1,2 . Lipids 2, 303–307 (1967). https://doi.org/10.1007/BF02532116

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  • DOI: https://doi.org/10.1007/BF02532116

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