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Clinical Chemistry 18: 662-666, 1972;
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Clinical Chemistry, Vol 18, 662-666, Copyright © 1972 by the American Association for Clinical Chemistry

Separation of Isoenzymes of Alkaline Phosphatase by Substrate—Gel Imprint after Electrophoresis on Cellulose Acetate

Douglas P. Rhone 1 and Florence M. Mizuno 1

1 Section of Biochemistry, Department of Pathology, Illinois Masonic Medical Center, 836 West Wellington Ave., Chicago, Ill. 60657.

Isoenzymes of alkaline phosphatase, separated by electrophoresis on cellulose acetate, were developed by a substrate—gel imprint. The gel was prepared in an alkaline buffer and contained beta-naphthyl acid phosphate, which was hydrolyzed to beta-naphthyl and phosphorus. The beta-naphthyl was coupled to the diazonium salt, Fast Violet B, and an insoluble red compound was formed on a cellulose acetate strip to mark the sites of enzyme activity. The electrophoretic mobilities of the isoenzymes were compared with those of serum proteins. Supporting data included thermostability and chemical inhibition (urea and phenylalanine) studies. This method was used to evaluate patterns in tissues and human sera.


Key Words: beta-naphthyl acid phosphate • Fast Violet B coupling • inhibition and thermostability • patterns with tissue extracts • normal values • patterns for newborns, mothers at term, and in liver disease

Submitted on February 16, 1972
Accepted on April 17, 1972






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Copyright © 1972 by the American Association for Clinical Chemistry.