Isolation and comparative studies of glycogen phosphorylase isoenzymes from lymphocytes and polymorphonuclear leucocytes.
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.
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
D000939:Epitopes; D007527:Isoenzymes; D006005:Phosphorylases