Malic dehydrogenase1
نویسندگان
چکیده
منابع مشابه
Malic Acid & Metabolic Acidosis
Label-MMAcid-Rev030410 BACKGROUND Ruminants are animals that have multiple stomachs to allow consumption and digestion of fibrous feedstuffs. Key to this digestive process is the bacterial breakdown of the fiber in the first stomach or rumen. The bacterial balance in the rumen can shift, allowing the ruminant to adapt to different diets. Ruminal bacteria convert fiber into lactate and volatile ...
متن کاملMalic Enzyme of Escherichia coli
The TPN+-specitk malic enzyme from Escherichia coli has been purified from malate-grown cells. An approximately loo-fold purified preparation is activated by NH4+ and K+ ions. The enzyme is inhibited by acetyl coenzyme A, oxalacetate, TPNH, and DPNH in an allosteric manner. Glycine at concentration ranges above 0.5 M has been shown to activate the enzyme as well as to desensitize it reversibly ...
متن کاملThe Inhibition of Fumarase and Malic Dehydrogenase
The competitive inhibition of malic dehydrogenase by /3-fluorooxaloacetate has been reported by Kun et al. (1). In addition to its inhibitory effect, /3-fluoro-oxaloacetate also oxidized reduced diphosphopyridine nucleotide enzymatically, but at a rate only 0.02% that of oxaloacetate. It was also shown (2) that fi-fluorooxaloacetate was a competitive inhibitor of glutamic-aspartic transaminase,...
متن کاملMalic Enzyme and Lipogenesis * by Edmund
10 Gershenson, S. I., J. Genet., 28, 297-313 (1933). 11TheYsX . YL-chromosome does not permit a decision as to whether YS and yL can conjoin intrachromosomally, even though this chromosome regularly conjoins with itself in Y8X.YL/O spermatocytes (Fig. 3i). Here "Ys" denotes with certainty only the Y8-fertility genes, for the "Ys" element itself (Fig. 3h) is morphologically unlike the short arm ...
متن کاملLimited proteolysis of maize NADP-malic enzyme.
The incubation of maize malic enzyme at 37 degrees C with trypsin at a ratio of 150:1 of malic enzyme to trypsin caused rapid and complete inactivation of enzyme activity. The inactivation was caused by fairly specific cleavage of the enzyme monomer (62 kDa) into 40 kDa and 20 kDa fragments. The intensity of 40 kDa band increased with the time of treatment of enzyme with trypsin from 2 to 30 mi...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1937
ISSN: 0306-3283
DOI: 10.1042/bj0311113