Abstract
Abstract A reproducible procedure for the large scale purification of pig heart supernatant malate dehydrogenase which yields up to 400 mg of homogeneous protein has been developed. The purity of the isolated enzyme is shown by acrylamide gel electrophoresis over a pH range from 4.9 to 9.2 as well as by detailed analysis of boundary spreading during sedimentation velocity experiments. Three enzymically active zones of enzyme were observed on gel electrophoresis at pH 4.9. Physical properties, including the partial specific volume, s20,w, apparent diffusion coefficient, molar extinction coefficient, and molecular weight, have been evaluated. Chemical determinations include a detailed quantitative amino acid analysis, amino end group analysis, and the preparation of peptide maps of tryptic digests of the enzyme. The results indicate that pig heart supernatant malate dehydrogenase is made up of two identical or very similar subunits.
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