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Clinical Chemistry 32: 1570-1573, 1986;
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Clinical Chemistry, Vol 32, 1570-1573, Copyright © 1986 by American Association for Clinical Chemistry

Alkaline phosphatase isoenzymes resolved by electrophoresis on lectin- containing agarose gel

WE Schreiber and L Whitta

With this electrophoretic method the liver, biliary, and bone isoenzymes of alkaline phosphatase are clearly separated on agarose gels. Wheat-germ lectin, incorporated in the gel matrix, binds the bone isoenzyme selectively, forming a precipitate near the origin. Neither liver nor biliary isoenzyme is affected. Activity staining with an indigogenic dye substrate reveals the liver isoenzyme migrating nearest the anode, followed by the biliary and bone isoenzymes. Results are generally similar to those of electrophoresis on cellulose acetate. However, the lectin-agarose gels better resolve the liver and bone isoenzymes, and heat treatment of samples is not required before electrophoresis.


The following articles in journals at HighWire Press have cited this article:


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 J. Clin. Endocrinol. Metab.Home page
H. Tobiume, S. Kanzaki, S. Hida, T. Ono, T. Moriwake, S. Yamauchi, H. Tanaka, and Y. Seino
Serum Bone Alkaline Phosphatase Isoenzyme Levels in Normal Children and Children with Growth Hormone (GH) Deficiency: A Potential Marker for Bone Formation and Response to GH Therapy
J. Clin. Endocrinol. Metab., July 1, 1997; 82(7): 2056 - 2061.
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Copyright © 1986 by the American Association for Clinical Chemistry.