Creatine kinase isoenzymes in Torpedo californica: absence of the major brain isoenzyme from nicotinic acetylcholine receptor membranes
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00354a012
Reference57 articles.
1. Brain isoenzyme of creatine kinase. I. Purification of rabbit enzyme and production of specific antibodies.
2. Peptide extraction by alkaline treatment is accompanied by rearrangement of the membrane-bound acetylcholine receptor from torpedo marmorata
3. A membrane-associated creatine kinase (EC 2.7.3.2) identified as an acidic species of the non-receptor, peripheralv-proteins inTorpedoacetylcholine receptor membranes
4. Creatine kinase activity in the Torpedo electrocyte and in the nonreceptor, peripheral v proteins from acetylcholine receptor-rich membranes.
5. Isolation and characterization of acetylcholine receptor membrane-associated (nonreceptor v2-protein) and soluble electrocyte creatine kinases.
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1. Sequence homology and structure predictions of the creatine kinase isoenzymes;Molecular and Cellular Biochemistry;1994-04
2. Creatine kinase in non-muscle tissues and cells;Molecular and Cellular Biochemistry;1994-04
3. Sequence homology and structure predictions of the creatine kinase isoenzymes;Cellular Bioenergetics: Role of Coupled Creatine Kinases;1994
4. Creatine kinase in non-muscle tissues and cells;Cellular Bioenergetics: Role of Coupled Creatine Kinases;1994
5. Intracellular compartmentation, structure and function of creatine kinase isoenzymes in tissues with high and fluctuating energy demands: the ‘phosphocreatine circuit’ for cellular energy homeostasis;Biochemical Journal;1992-01-01
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