Macro XXXX kinase type 1 with electrophoretic mobility identical to that of the MB isoenzyme.

@entity1 @entity9055 @entity908 @entity16410 @entity911 @entity583
We describe the case of an elderly @entity1 whose symptoms and electrocardiographic pattern initially suggested acute @entity583 . The value for total serum @entity908 kinase (EC 2.7.3.2; CK) was 737 U/L (reference interval: 22-269 U/L), and electrophoresis for CK isoenzymes demonstrated two bands, the more anodal migrating to the CK-MB region and the second migrating between the CK-MB and CK-MM regions. The above-normal total CK and electrophoretic pattern persisted during her 11-day hospital course. The QuiCK-MB (International Immunoassay Labs.) and Tandem-E CK-MB (Hybritech) immunoassays, however, showed CK-MB mass measurements within the normal range. In further investigation with a mixture of patient's serum and human-serum-based control containing all CK isoenzymes, the electrophoretic mobility of only @entity9055 was altered, proving that the patient had antibody to the B unit of CK in her serum. Immunofixation revealed the more anodal band to be a CK-IgA lambda complex, and the more cathodal band, a CK-IgG kappa complex. Mixing the patient's serum with polyclonal antibody specific for @entity9055 slowed the electrophoretic mobility of only the more anodal band. Polyclonal antibody specific for @entity16410 had no effect on either band. Evidently, this @entity1 had two different types of macro CK type 1, both containing @entity9055 . We conclude that macro CK type 1 can mimic CK-MB and be a source of @entity911 .
