A membrane-bound creatine phosphokinase in fragmented sarcoplasmic reticulum.

Abstract Fragmented sarcoplasmic reticulum was isolated from rabbit skeletal muscle and creatine phosphokinase activity was measured; 0.2 to 1.16 units of creatine-P kinase per mg of fragmented sarcoplasmic reticulum protein were found. The activity was inhibited by dinitrofluorobenzene, a known inhibitor of creatine-P kinase, and had Km values similar to those measured for crystalline enzyme. Since the activity diasppeared from the supernatant upon centrifugation, the creatinine-P kinase is bound to the membranous fraction of the fragmented microsomal preparation. However, it was not present on the mitochondrial fraction from the same muscle homogenate. The creatine-P kinase of the fragmented sarcoplasmic reticulum preparation represents approximately 1% of the total activity in muscle and may be significant as a localized source of ATP for calcium transport processes during muscle relaxation.

• Publication year

  1970

• Venue

  Journal of Biological Chemistry

• Publication date

  1970-03-25

• Fields of study

  Biology, Medicine

• Identifiers
  DOI 10.1016/s0021-9258(18)63242-9PMID 5442823
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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