Abstract
Improved, and relatively simple procedures are described for the purification of human and canine creatine kinase isoenzymes with much higher yields (30 to 60%) and purity (450 kU/g) than previously possible. Contaminant albumin was removed from the MB preparation by albumin antibodies attached to Sepharose-4B. All isoenzyme preparations exhibited a single protein band on SDS gel electrophoresis. Using specific antisera to the isoenzymes and albumin the preparations were shown to be immunochemically pure and to give reliable results in a radioimmunoassay. © 1982.