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Creatine Kinase in Human Tissues
David M. Dawson, MD;
I. Howard Fine, MD
Arch Neurol. 1967;16(2):175-180.
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| Since this article does not have an abstract, we have provided the first 150 words of the full text PDF and any section headings. |
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ANUMBER of enzymes are known to occur in the body in one or more distinct forms, usually called isozymes.1-3 The molecular basis for this phenomenon is known in the case of two soluble enzymes: creatine kinase and lactic dehydrogenase. In both cases the isozymes are formed of polymers of two kinds of subunits, each of which is under separate genetic control.
Both enzymes, more particularly lactic dehydrogenase, have come under intensive investigation in the past few years, in part because of the inherent interest of the phenomenon of isozyme structure, and also because it has been hoped that the pattern of isozymes in a cell would give information or insight of clinical value.
This paper reports the isozyme types and normal levels of creatine kinase from human tissues obtained at autopsy. These values are of interest because of the widespread use of serum creatine kinase activity as an indicator
. . . [Full Text PDF of this Article]
Author Affiliations
Boston
From the Harvard Neurological Unit Boston City Hospital and the Department of Neurology, Harvard Medical School (Dr. Dawson); and the Boston University School of Medicine (Dr. Fine).
Footnotes
Submitted for publication July 26, 1966; accepted Sept 14.
Reprint requests to the Neurological Unit, Boston City Hospital, Boston (Dr. Dawson).
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