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. 1970 Dec;120(3):589–600. doi: 10.1042/bj1200589

Brain adenosine 5′-triphosphate–creatine phosphotransferase. Purification, thiol group reactivity and the amino acid sequence around the reactive thiol groups

R S Atherton 1, J F Laws 1, B J Miles 1, A R Thomson 1
PMCID: PMC1179640  PMID: 5499971

Abstract

1. The purification of creatine kinase (ATP–creatine phosphotransferase, EC 2.7.3.2) from ox brain by a method that is quicker, simpler and gives much higher yields than other published procedures is described. 2. Stoicheiometric inhibition studies with iodoacetate showed that the enzyme, like that from muscle, has two reactive thiol groups that are essential for enzyme activity. 3. The amino acid sequence around the essential thiol groups was determined and found to be virtually identical with that in creatine kinases from rabbit and ox muscle, and very similar to that found in arginine kinase; the evolutionary significance of this is discussed. 4. The identification of DNS-amino acids on thin layers of silica gel was found to have, in many cases, distinct advantages over that on polyamide layers.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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