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- W1538182712 abstract "Abstract An investigation of the properties of purifed rabbit muscle amylo -1,6- glucosidase/oligo -1,4 → 1,4- glucantransferase was conducted utilizing a modification of the iodine-complex spectrum of amylopectin and glycogen phosphorylase limit dextrin. A rapid and convenient method of assaying for the transferase activity was developed to study its activity. The pH optimum of the transferase differs from that of amylo- i ,6-glucosidase, which is associated with it throughout purification. Tris, which both inhibits and shifts the pH optimum of the glucosidase, has little or no effect on the trasnferase. MoO42−, on the other hand, inhibits the transferase but not the glucosidase. The action of the transferase on amylopectin is not dependent on the glucosidase. With glycogen phosphorylase limit dextrin, however, the modification in iodine color is a product of both glucosidase and transferase action. Assay of tissue extracts utilizing the modification of the iodine-complex spectrum of phosphorylase limit dextrin was found to be specific for glucosidase-transferase activity. The differences in properties of the glucosidase and the transferase suggests that they have different active sites even though they are apparently associated with the same protein molecule." @default.
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- W1538182712 date "1970-08-01" @default.
- W1538182712 modified "2023-09-24" @default.
- W1538182712 title "An investigation of the properties of rabbit muscle" @default.
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- W1538182712 doi "https://doi.org/10.1016/0005-2744(70)90207-x" @default.
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