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- W2013756415 abstract "Abstract 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 are characteristic of a sequential reaction mechanism. The Km values of starch phosphorylases III, IV and V in the direction of polysaccharide degradation for starch, glycogen, amylopectin and amylose are greater than those of starch phosphorylases I and II. All the multiple forms have shown similar affinity for orthophosphate. The Km values of starch phosphorylases III, IV and V for glucose-1-phosphate are much greater than those of starch phosphorylases I and II. Mrs of starch phosphorylases I, II, III, IV and V determined by gel filtration chromatography are 180 000, 210 000, 180 000, 210 000 and 330 000, respectively. Aromatic amino acids, phenolic compounds and heavy metal ions inhibit the phosphorylase reaction." @default.
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- W2013756415 date "1996-02-01" @default.
- W2013756415 modified "2023-10-08" @default.
- W2013756415 title "Multiple forms of starch phosphorylase from Sorghum leaves" @default.
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- W2013756415 doi "https://doi.org/10.1016/0031-9422(95)00709-1" @default.
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