Partial characterization, properties, and clinical significance of a lactate dehydrogenase-immunoglobulin A kappa...

The existence of a lactate dehydrogenase-immunoglobulin A kappa complex was demonstrated as a marked increase of lactate dehydrogenase activity at the lactate dehydrogenase-3 band in the agar-agarose gel-electrophoresis pattern of sera from seven patients from an unselected group of 21 800 patients. The complex was isolated, in an almost pure form, by gel filtration and affinity chromatography, from the serum of a patient with circulating hepatitis B surface antigen. The complex had a relative molecular mass (Mr) of approximately 445 000 as determined by gel filtration. Electrophoresis in sodium dodecyl sulfate in the absence of reducing agents showed the presence of two subunit bands with Mr 170 000 and 34 000. We therefore propose that the native complex consists of one monomeric immunoglobulin A kappa linked to two tetrameric lactate dehydrogenase molecules. The enzymic activity of the complex is probably from lactate dehydrogenase isoenzyme-5.