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Two major and three minor peaks of starch phosphorylase activity from leaves of Sorghum vulgare have been separated by chromatography on DEAE-cellulose and further purified using Sephadex G-200 chromatography. The initial velocity patterns of the reaction between glucose-1-phosphate and various primers, viz. starch, glycogen, amylopectin and amylose, determined as a function of substrate concentration...
Starch phosphorylase (EC.2.4.1.1.) from the filaments of Cuscuta reflexa has been purified using (NH 4 ) 2 SO 4 fractionation, ion-exchange chromatography using DEAE cellulose and gel filtration through Sephadex G-200. The enzyme preparation is estimated to be about 85-90% pure as revealed by native polyacrylamide gel electrophoresis. The native M r of the enzyme...
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