title: Isolation and comparative studies of glycogen phosphorylase isoenzymes from lymphocytes and polymorphonuclear leucocytes.
abstract: Two glycogen phosphorylase isoenzymes have been identified in pig lymphocytes and polymorphonuclear leucocytes by DEAE cellulose chromatography. Both isophosphorylases have been further purified by affinity chromatography on Sepharose-AMP to almost homogeneity. The purified isophosphorylases were composed of subunits of molecular weight similar to the muscle and liver monomers. Isophosphorylase I was more related to the liver enzyme than isophosphorylase II based on immuno-inhibition experiments. Both isoenzymes were markedly different from liver and muscle phosphorylases in their activation by AMP, sodium sulfate and 1,2-dimethoxyethane.
mesh_terms: D000818:Animals; D002846:Chromatography, Affinity; D002848:Chromatography, DEAE-Cellulose; D004789:Enzyme Activation; D000939:Epitopes / Q000276:immunology; D007527:Isoenzymes / Q000097:blood* / Q000276:immunology / Q000302:isolation & purification; D008099:Liver / Q000201:enzymology; D008214:Lymphocytes / Q000201:enzymology*; D009132:Muscles / Q000201:enzymology; D009504:Neutrophils / Q000201:enzymology*; D006005:Phosphorylases / Q000097:blood* / Q000276:immunology / Q000302:isolation & purification; D011817:Rabbits; D013552:Swine
chemical_list: D000939:Epitopes; D007527:Isoenzymes; D006005:Phosphorylases