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Clinical Chemistry 39: 1404-1407, 1993;
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Clinical Chemistry, Vol 39, 1404-1407, Copyright © 1993 by American Association for Clinical Chemistry

Wheat germ lectin affinity electrophoresis of serum alkaline phosphatase with commercially available agarose gels

M Mattiazzo and I Ramasamy
Department of Biochemistry, Repatriation Hospital, Daw Park, Australia.

We have modified a commercially available procedure involving precast agarose gels (Paragon Isopal System) to measure alkaline phosphatase (EC 3.1.3.1) isoenzymes. Including wheat germ lectin in the equilibration buffer improved the resolution of the bone and liver isoenzymes. Unlike previously described wheat germ lectin affinity electrophoresis methods, the procedure measures bone, liver, and biliary isoenzymes in a single step. There was good correlation between the affinity electrophoresis and the neuraminidase preincubation methods for the measurement of bone (r = 0.958) and liver (r = 0.962) alkaline phosphatase isoenzymes. However, the affinity electrophoresis method also quantified minor isoenzyme fractions that were poorly resolved by the neuraminidase method. The method is technically simple, reproducible, and capable of rapid handling of large workloads.


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.
[Abstract] [Full Text] [PDF]


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