[Distribution of the action of creatine kinase, AMP-aminohydrolase and ATPase,and absorption of Ca+n microsomal fractions of skeletal muscles].
The microsomal fraction of the rabbit skeletal muscles contains structures which absorb Ca2+ and where ATPase-aminohydrolase activities are pronounced. Electrophoresis of this fraction in the saccharose density gradient results in separation of a considerable amount of soluble proteins including creatine kinase, as a high ATPase activity and absorbing Ca2+ to an inconsiderable extent. The activity of creatine kinase in the microsomal fraction of the rabbit and rat skeletal muscles is not so high to provide for ATP regeneration from creatine phosphate in the amount sufficient for any considerable transport of Ca2+. In the microsomal fraction of the myocardium, as distinct from the skeletal muscles creatine kinase is strongly bound with its structural components and is not separated by electrophoresis.
D000659:AMP Deaminase / Q000378:metabolism*; D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000818:Animals; D001665:Binding Sites; D001693:Biological Transport, Active; D002118:Calcium / Q000378:metabolism*; D002458:Cell Fractionation; D003402:Creatine Kinase / Q000378:metabolism*; D008861:Microsomes / Q000378:metabolism*; D009132:Muscles / Q000378:metabolism*; D009206:Myocardium / Q000378:metabolism; D009709:Nucleotide Deaminases / Q000378:metabolism*; D009928:Organ Specificity; D011485:Protein Binding; D011817:Rabbits
D003402:Creatine Kinase; D009709:Nucleotide Deaminases; D000659:AMP Deaminase; D000251:Adenosine Triphosphatases; D002118:Calcium