Enzyme synthesis and adaptation of hepatic “malic” enzyme

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Regulation of hepatic malic enzyme mRNAs during development.

Previous studies in vivo have demonstrated that in neonatal and adult rats hepatic malic enzyme expression is controlled at the pretranslational level by dietary and hormonal factors [ 1, 21. However, in order to demonstrate that particular effectors have a direct effect on gene expression in liver cells, techniques in vitro, such as the use of primary cultures of non-proliferating rat hepatocy...

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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 ...

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Regulation of mitochondrial malic enzyme synthesis in mouse brain.

In a previous study [Bernstine, E.G. (1979) J. Biol. Chem. 254, 83-87] it was shown that inbred strains of mice fall into two classes based on the specific activity of mitochondrial malic enzyme [L-malate:NADP+ oxidoreductase (oxaloacetate-decarboxylating), EC 1.1.1.40] in brain. In this report we demonstrate differences between high- and low-activity strains in the development of enzyme activi...

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Malic 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 ...

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Limited 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: 1972

ISSN: 0306-3283

DOI: 10.1042/bj1300076pb