[The characteristics of the interaction of glycogenolytic enzymes with glycogen in endothermic and ectothermic animals].
It has been shown that the dependence of glycogenphosphorylase kinase activity on the quantity of glycogen added corresponds to the glycogenphosphorylase saturation curve by glycogen obtained during investigation of complex formation with the muscle glycogenphosphorylase of the animals: rat, frog Rana temporaria and fish Raja clavata under identical conditions. We suggest that glycogenolytic enzymes organize regular structure on glycogen particle. Glycogenphosphorylases of heat-loving animals have high affinity to glycogen that is accounted for necessity to keep the structure in natural conditions.
Serebrenikova
T P
TP
Shmelev
V K
VK
D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D001833:Body Temperature Regulation / Q000502:physiology*; D004347:Drug Interactions; D006003:Glycogen / Q000378:metabolism*; D009132:Muscles / Q000201:enzymology; D010764:Phosphorylase Kinase / Q000378:metabolism*; D006005:Phosphorylases / Q000378:metabolism*; D011817:Rabbits; D011896:Rana temporaria; D012860:Skates, Fish; D013045:Species Specificity
D000255:Adenosine Triphosphate; D006003:Glycogen; D006005:Phosphorylases; D010764:Phosphorylase Kinase
Osobennosti vzaimodeĭstviia fermentov glikogenoliza s glikogenom u éndotermnykh i éktotermnykh zhivotnykh.