Evidence for three enzymatic activities in one electrophoretic band of 3-phosphoglycerate mutase from red cells.
Electrophoresis of 3-phosphoglycerate mutase from erythrocytes of man and several animal species has been performed on cellulose acetate strips. In most cases the electrophoretic pattern of this enzymatic activity shows three bands. 2,3-diphosphoglycerate phosphatase and diphosphoglycerate mutase from erythrocytes of the same species have been revealed after migration during the same electrophoresis. We found that the band of 2,3-diphosphoglycerate phosphatase and the band of diphosphoglycerate mutase activities migrate at the same level as one of the bands corresponding to 3-phosphoglycerate mutase. Here, we discuss the possible existence of a single molecule carrying three enzymatic activities.
D000818:Animals; D001731:Bisphosphoglycerate Mutase / Q000097:blood; D004163:Diphosphoglyceric Acids; D004588:Electrophoresis, Cellulose Acetate; D004912:Erythrocytes / Q000201:enzymology*; D006041:Goats; D006736:Horses; D006801:Humans; D008974:Mollusca; D010736:Phosphoglycerate Mutase / Q000097:blood*; D010744:Phosphoric Monoester Hydrolases / Q000097:blood; D010770:Phosphotransferases / Q000097:blood*; D051381:Rats
D004163:Diphosphoglyceric Acids; C019794:bisphosphoglycerate phosphatase; D010770:Phosphotransferases; D010744:Phosphoric Monoester Hydrolases; D010736:Phosphoglycerate Mutase; D001731:Bisphosphoglycerate Mutase