Clinical Chemistry
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Clinical Chemistry 38: 507-511, 1992;
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Clinical Chemistry, Vol 38, 507-511, Copyright © 1992 by American Association for Clinical Chemistry

Prevalence and properties of the intestinal alkaline phosphatase identified in serum by cellulose acetate electrophoresis

WC Griffiths, PD Camara, M Rosner, R Lev and EM Brooks
Roger Williams Hospital, Department of Pathology and Laboratory Medicine, Providence, RI.

We investigated the prevalence and characteristics of intestinal alkaline phosphatase (ALP; EC 3.1.3.1) identified in human serum by cellulose acetate electrophoresis in 8% of fasting serum samples from hospital patients (n = 500) and in 35% of fasting serum samples from patients with diabetes mellitus (n = 106; not differentiated between types 1 and 2). The intestinal ALP electrophoretic band was usually heterogeneous and contained two major subtypes of ALP. Isoelectric focusing of intestinal-ALP-positive serum treated with levamisole and neuraminidase (EC 3.2.1.18) revealed two distinct regions of enzymatic activity that comigrated with ALP extracted from small intestinal and colonic mucosa. Anodic intestinal ALP was resistant to treatment with levamisole and neuraminidase and comigrated with ALP from small intestinal mucosa. The more-cathodic intestinal ALP, which comigrated with ALP from colonic mucosa, was completely inhibited by levamisole and converted by neuraminidase to a species with a more basic pI than that of neuraminidase-digested tissue-nonspecific form. This component of intestinal ALP may be of vascular origin.




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Copyright © 1992 by the American Association for Clinical Chemistry.