Richard G. Wolfe

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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(More)
At pH 8.0 in 0.05 M Tris-acetate buffer at 25 degrees C, homogeneous supernatant malate dehydrogenase exhibits substrate activation by L-malate. The turnover number, Michaelis constant for L-malate, and Michaelis constant for NAD are: 0.46 X 10(4) min(-1), 0.036 mM, and 0.14 mM, respectively, for nonactivated enzyme and 1.1 X 10(4) min(-1), 0.2mM, and 0.047(More)
A total of 35 pigs were obtained by cesarean section, placed in individual sterile isolators, and randomly allotted to treatment groups. Thirty pigs received purified, isoenergetic liquid diets containing 2 or 32% butterfat (dry matter basis) and were killed at 1, 7, or 21 days of age. Five pigs were killed at 2 hours post delivery and received no diet.(More)