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CREATINE KINASE FROM BRAIN: KINETIC ASPECTS
Author(s) -
Dawson D. M
Publication year - 1970
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1970.tb00502.x
Subject(s) - creatine kinase , creatine , enzyme , phosphocreatine , substrate (aquarium) , biochemistry , glycolysis , phosphate , chemistry , mitochondrion , biology , endocrinology , energy metabolism , ecology
Abstract— Creatine kinase derived from rabbit brain has been re‐examined with respect to its kinetic features. The enzyme from brain has lower Michaelis constants for both ADP and creatine phosphate than does the enzyme from rabbit muscle. Substrate inhibition by excess creatine phosphate occurs at a concentration approximating that found in the tissue. The enzyme from muscle is less sensitive to substrate inhibition. The crude mitochondrial fraction from rat brain was centrifuged in a sucrose density gradient and the distribution of enzymatic activities among the subfractions was determined. The distribution of creatine kinase resembled that of two glycolytic enzymes; no evidence for a mitochondrial localization was found.