Fluorescence of Glycogen Phosphorylase b

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Fluorescence of glycogen phosphorylase b. Structural transitions and energy transfer.

The fluorescence properties of glycogen phosphorylase b and its apoenzyme are described. At neutral pH the enzyme has two fluorescence bands: one caused by the protein moiety (maximum at 335 nm, quantum yield 0.12) and the other associated with the cofactor, pyridoxal 5’-phosphate (maximum at 535 nm, quantum yield 0.012). Pyridoxal5’-phosphate can be regarded as a native reporter group of phosp...

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ORDERED MECHANISM OF BINDING OF PHOSPHORYLASE KINASE AND GLYCOGEN PHOSPHORYLASE b TO GLYCOGEN

The kinetics of the interaction of rabbit skeletal muscle phosphorylase kinase with glycogen has been studied using turbidimetric method (40 mM Hepes, pH 6.8, and 8.2; 20◦C). The binding of phosphorylase kinase with glycogen occurs only in the presence of Ca and Mg . According to the kinetic data, phosphorylase b favors the binding of phosphorylase kinase with glycogen. This conclusion is suppo...

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Synthesis of heterocyclic N-(b-D-gluco of glycogen phosphorylase

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Two active isoforms of bovine liver phosphorylase with distinct subunit composition have previously been purified (Cámara Artigas, A., Barón, C. and Parody-Morreale, A. Prot. Express. Purif. 1994, 5, 157), one showing three SDS-PAGE polypeptide bands (molecular mass = 97, 55 and 40 kDa) and the other showing just one (molecular mass = 97 kDa). A molecular mass of 200 kDa has been determined for...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1971

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(18)62413-5