Abstract
Two isoenzyme of inorganic alkaline PPase from corn leaves were obtained and partially purified by ammonium sulphate precipitation, DEAE-Sephadex A-50 chromatography and gel filtration on Sephadex G 100. The specific activity of one isoenzyme was 356.4 units/mg protein and represented a 307.1-fold enrichment relative to the crude extract, with 24 % yield. The specific activity of the second isoenzyme was 1/6 of that of the PPase A activity; it represented a 51.7-fold enrichment, with 6.7% yield. Both enzymes exhibited maximum activity at pH 8.8 and at the Mg 2+ /PPi ratio of 5. They differed only in their electrophoretic mobility and in their susceptibility to urea and thermal denaturation.
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