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Charles P. Turley
University of Arkansas for Medical Sciences Little Rock

JAMA. 1981;245(8):822-823.

	Since this article does not have an abstract, we have provided the first 150 words of the full text PDF and any section headings.

To the Editor.—

We would like to comment on the article by C. Jack Bark, MD (1980;24:2058), in which he postulates that a creatine kinase (CK) isoenzyme migrating cathodically to the CK-MM band represents mitochondrial CK.

Although it has been generally accepted that the commercially produced reagents inhibit adenylate kinase (AK) activity in CK electrophoretic isoenzyme separations, experience in our laboratory has shown otherwise. Using the same system as Bark, we have detected the presence of bands cathodic to CK-MM that were caused by uninhibited AK.₁ We have also found cathodically migrating bands that are susceptible to antibodies directed against the M-subunit of CK, suggesting the possibility of altered electrophoretic mobility caused by binding of an exogenous substance or genetic variability, without affecting the binding site. We would therefore caution against interpreting the cathodic CK bands as being of mitochondrial origin, unless definitive additional studies including the use of . . . [Full Text PDF of this Article]

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