Microheterogeneity of the malate dehydrogenase from several sources.
Different homogeneously purified cytosolic malate dehydrogenases gave, on isoelectric focusing, several active bands. The phenomenon could not be assigned to differences in their molecular weights or to alterations in the enzyme preparations during the purification procedure. Resolution of the multiple malate dehydrogenase active bands was achieved by chromatofocusing. The aged isolated subforms always yielded the original electrofocusing pattern. This fact suggests that conformational isomerism is a likely explanation for the charge heterogeneity of the enzymes studied.
D000818:Animals; D002645:Chickens; D002845:Chromatography; D002850:Chromatography, Gel; D003600:Cytosol / Q000201:enzymology; D006168:Guinea Pigs; D007525:Isoelectric Focusing; D008099:Liver / Q000201:enzymology; D008291:Malate Dehydrogenase / Q000302:isolation & purification*; D008970:Molecular Weight; D009132:Muscles / Q000201:enzymology; D011487:Protein Conformation
D008291:Malate Dehydrogenase