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Electrophoretic Behaviour of an Aminopeptidase of Human Tissues and Serum

Nature volume 197, pages 800–801 (1963)Cite this article

Abstract

A SERUM aminopeptidase* (LAP) that hydrolyses L-leucyl-β-naphthylamide migrates as a single component to the α1-globulin region in the electrophoretic pattern of normal serum and the serum of the first and second trimesters of pregnancy. Additional components of LAP which migrate to other areas have been found in the serum of many patients with hepatobiliary and pancreatic diseases and in the third trimester of pregnancy1–3. The origin of these ‘isoenzymes’ of serum LAP was sought in an examination of the electrophoretic mobility of LAP from various tissues which exhibited high specific activity of this enzyme.

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Authors and Affiliations

  1. Yamins Laboratory for Surgical Research, Beth Israel Hospital, and Departments of Surgery, Beth Israel Hospital and Harvard Medical School, Boston, Mass.

    EDGAR E. SMITH & ALEXANDER M. RUTENBURG

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  1. EDGAR E. SMITH
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  2. ALEXANDER M. RUTENBURG
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SMITH, E., RUTENBURG, A. Electrophoretic Behaviour of an Aminopeptidase of Human Tissues and Serum. Nature 197, 800–801 (1963). https://doi.org/10.1038/197800a0

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