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

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Abstract
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 β-naphthyl acid phosphate, which was hydrolyzed to β-naphthyl and phosphorus. The β-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.

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