The electrophoretic separations of some human and pig liver enzymes on cellulose acetate and Cellogel were investigated, with reference to their joint occurrence in serum of patients undergoing treatment by extracorporeal pig liver perfusion. In every case it was possible to distinguish between the human and pig enzymes. Pig lactate dehydrogenase isoenzymes occupy a position slightly anodic to the corresponding human bands. The aspartate transaminase band of human is more anodic than that of pig, but their cathodic bands have the same mobility. Alanine transaminase of both human and pig liver extract is shown to exist as two bands each towards the anode. The faster moving human band is more anodic than the corresponding pig band, while the other human band is less anodic. Sorbitol dehydrogenase, alkaline phosphatase, and ornithine carbamoyltransferase all exist as one band each. Human sorbitol dehydrogenase is more cathodic than the pig enzyme, human alkaline phosphatase more anodic than the pig enzyme, while human ornithine carbamoyltransferase is less anodic than the pig enzyme.
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