Chromatographic behavior of immunoglobulin-bound creatine kinase on DEAE-Sephadex A-50.
We investigated the chromatographic behavior of CK isoenzymes and immunoglobulin-bound macro-CK by discontinuous gradient elution from DEAE-Sephadex A-50 at pH 7 and 8. In four of five patients with macro-CK, the macro-CK was eluted with the MB buffer at pH 8, but a significant portion of the complex was eluted with the MM buffer at pH 7, in a region between CK-MM and CK-MB. In the fifth patient, the macro-CK was eluted with the MB buffer at both pH values. The immunoglobulin patterns of all five patients and of normal serum showed that IgG and IgM are eluted mainly with the MM and MB buffers, respectively, at both pH values, whereas IgA is eluted mainly with the MB buffer at pH 8, but at pH 7, shows a significant shift similar to that of macro-CK. These characteristic patterns allowed the identification of the immunoglobulin in macro-CK as IgA in the first four patients, and as IgM in the fifth patient.
D000328:Adult; D000368:Aged; D002852:Chromatography, Ion Exchange; D003402:Creatine Kinase / Q000097:blood*; D005260:Female; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007120:Immunochemistry; D007070:Immunoglobulin A / Q000032:analysis; D007074:Immunoglobulin G / Q000032:analysis; D007075:Immunoglobulin M / Q000032:analysis; D007136:Immunoglobulins / Q000032:analysis*; D007527:Isoenzymes; D008875:Middle Aged; D011485:Protein Binding
D007070:Immunoglobulin A; D007074:Immunoglobulin G; D007075:Immunoglobulin M; D007136:Immunoglobulins; D007527:Isoenzymes; D003402:Creatine Kinase