title: Sub-unit structure of soluble and mitochondrial malic enzyme: demonstration of human mitochondrial enzyme in human-mouse hybrids.
abstract: 1. Malic enzyme has been examined by starch-gel electrophoresis in human cultured fibroblasts and in 60 brain samples. The polymorphism of MEM has been confirmed and the electrophoretic pattern suggests that this enzyme, like MES, is a tetramer. 2. The appearance of the soluble and mitochondrial malic enzymes in mouse and Chinese hamster is described, and the identity of the enzymes in man, mouse and hamster has been established from a study of interspecific somatic cell hybrids. In man and in hamster MES migrates anodal to MEM, whereas in the mouse MES is relatively less anodal than MEM. 3. Segregation of human enzymes in human--mouse and human--hamster somatic cell hybrids confirms the synteny of MES and PGM3. Data from human--mouse hybrids suggest that MEM is probably not syntenic with MES is probably not syntenic with MES in man, nor is it syntenic with GPI.
mesh_terms: D000818:Animals; D001921:Brain / Q000201:enzymology; D002875:Chromosomes; D004592:Electrophoresis, Starch Gel; D004792:Enzyme Precursors / Q000378:metabolism; D005796:Genes; D006801:Humans; D006822:Hybrid Cells / Q000201:enzymology; D007621:Karyotyping; D008291:Malate Dehydrogenase / Q000235:genetics / Q000378:metabolism; D051379:Mice; D008928:Mitochondria / Q000201:enzymology*; D008970:Molecular Weight; D011110:Polymorphism, Genetic; D013045:Species Specificity
chemical_list: D004792:Enzyme Precursors; D008291:Malate Dehydrogenase