title: [Glycogen phosphorylase of skeletal muscles].
abstract: A review is given on the affinity modification of pyridoxal phosphate and AMP-binding sites as well as on the chemical modification of essential amino acid residues of phosphorylase (histidine residue of the substrate-binding site and cysteine residue of the coenzyme-binding site). The role of allosteric effectors (AMP and glucose-6-phosphate) and functionally important centers of the protein in conformational transitions of rabbit muscle phosphorylase b is discussed. The kinetic properties of rabbit and bovine muscle phosphorylase are compared. Bovine muscle phosphorylase is shown to be a partly phosphorylated form of the enzyme. Some peculiarities of the pH-dependence of kinetic behaviour of the hybrid form of the bovine muscle enzyme are discussed.
mesh_terms: D000818:Animals; D001665:Binding Sites; D007700:Kinetics; D009119:Muscle Contraction; D009132:Muscles / Q000201:enzymology*; D006005:Phosphorylases / Q000378:metabolism*
chemical_list: D006005:Phosphorylases
vernacular_title: Glikogenfosforilaza skeletnykh myshts.