Glycogen metabolizing enzymes in brain.
Three enzymes, glycogen phosphorylase, glycogen synthase, and phosphoglucomutase were evaluated in subcellular fractions and in brain regions. Also the development of each of these enzymes was evaluated in whole brain homogenates. Each enzyme increased during the first three weeks of post partum in a manner that is similar to the development of glycolytic enzymes during this period. The specific activity of each enzyme in various subcellular fractions indicated that the enzymes were primarily soluble. Also unlike the glycolytic enzyme phosphoglycerate kinase, the glycogen metabolizing enzymes had a lower specific activity in synaptosomes than in particle free supernatant fractions of homogenates. Regarding regional distribution small (less than twofold) but significant differences were seen between different brain areas. An inverse relationship between the glycogen metabolizing enzymes and hexokinase was observed, that is, regions highest in glycogen synthase and glycogen phosphorylase were lowest in hexokinase and regions highest in hexokinase were lowest in the glycogen metabolizing enzymes.
D000367:Age Factors; D000818:Animals; D001921:Brain / Q000201:enzymology*; D006003:Glycogen / Q000378:metabolism*; D006006:Glycogen Synthase / Q000032:analysis; D006593:Hexokinase / Q000032:analysis; D008297:Male; D010733:Phosphoglucomutase / Q000032:analysis; D006005:Phosphorylases / Q000032:analysis; D051381:Rats; D011919:Rats, Inbred Strains
D006003:Glycogen; D006005:Phosphorylases; D006006:Glycogen Synthase; D006593:Hexokinase; D010733:Phosphoglucomutase