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Clinical Chemistry, Vol 26, 1816-1820, Copyright © 1980 by American Association for Clinical Chemistry
H Yuu, S Ishizawa, Y Takagi, K Gomi, O Senju and T Ishii
We describe three cases in which creatine kinase (CK, EC 2.7.3.2) was linked to immunoglobulin in serum. In this study, its prevalence was 0.8%. Enzyme-immunofixation electrophoresis revealed that the heavy chain of CK-linked immunoglobulins was of class alpha in all cases. The light-chain type was identified as lambda in two cases and as both lambda and kappa in one case. The complexes were dissociated at pH 3.4 and re-formed with CK isoenzymes MM and MB at pH 7.4. The complex fraction obtained by gel filtration was not inhibited by anti-CK-M antibodies. Treatment of the serum with urea after heating shows residual CK-MM activity; in contrast, normal CK activity disappeared entirely after this treatment. The present study suggests that CK- linked immunoglobulins may be one of the circulating immune complexes and must be distinguished from other macro-CK in the strict sense. The results obtained show that the presence of the complexes results in false-positive CK-B activity in the immuno-inhibition test, and they may provide interesting insights into the mode of binding of the CK- linked immunoglobulins.
The following articles in journals at HighWire Press have cited this article:
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L. A. Lipsitz, F. C. Pluchino, and J. Y. Wei The Prevalence and Prognosis of Minimally Elevated Creatine Kinase--Myocardial Band Activity in Elderly Patients With Syncope Arch Intern Med, July 1, 1987; 147(7): 1321 - 1323. [Abstract] [PDF] |
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