Abstract
A SPARTIC aminopherase from skeletal or heart muscle is readily dissociable and catalyses the transamnination between l-aspartic and pyruvic acids in the presence of a dialysable co-enzyme1. Concentrates of this co-aminopherase have been prepared from pig heart by us and the substance has been shown to be acid-labile2. Glutamic aminopherase is not inactivated by dialysis. Attempts of Cohen3 and L'nard and Straub to activate this enzyme with thermostable factors are based upon misinterpretation of the suggestion that glutamic aminopherase might contain a difficultly dissociable prosthetic group similar to co-aspartic-aminopherase1.
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BRAUNSTEIN, A., KRITZMANN, M. Co-Aminopherase, Co-Decar-Boxylase and Pyridoxal. Nature 158, 102–103 (1946). https://doi.org/10.1038/158102a0
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DOI: https://doi.org/10.1038/158102a0
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