Search Results - "Fang, T.K"

Characterization of two glutamate decarboxylase cDNA clones from Arabidopsis by Turano, F.J. (USDA, ARS, Climate Stress Laboratory, Beltsville, MD.), Fang, T.K

“…Two distinct cDNA clones encoding for the glutamate decarboxylase (GAD) isoenzymes GAD1 and GAD2 from Arabidopsis (L.) Heynh. were characterized. The open…”
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Multiple excitation in photoionization using B-splines by Chang, T.N., Fang, T.K.

“…We present a review of a few recent applications of three B-spline-based methods to atomic photoionization dominated by multiple excitation for both single and…”
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Regulation of the pyruvate dehydrogenase complexes in plants by Randall, D D, Miernyk, J A, Fang, T K, Budde, R J, Schuller, K A

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Acetyl-coenzyme A can regulate activity of the mitochondrial pyruvate dehydrogenase complex in situ by Budde, R.J.A. (University of Missouri, Columbia, MO), Fang, T.K, Randall, D.D, Miernyk, J.A

“…In vitro, the pyruate dehydrogenase complex is sensitive to product inhibition by NADH and acetyl-coenzyme A (CoA). Based upon Km and Ki relationships, it was…”
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Effect of positive-energy orbitals on the photoionization cross sections and oscillator strengths of He and divalent atoms by Chang, TN, Fang, TK

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Electron transport in purified glyoxysomal membranes from castor-bean endosperm by Fang, T.K. (George Washington Univ., Washington D.C. (USA). Dept. of Biological Sciences), Donaldson, R.P, Vigil, E.L

“…Glyoxysomes isolated from castor-bean (Ricinus communis L.) endosperm were treated with water, 0.2 M KCl, 1 M KCl, or 0.1 M Na2CO3. Glyoxysomal sacs, i.e…”
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beta-Oxidation and glyoxylate cycle coupled to NADH: cytochrome c and ferricyanide reductases in glyoxysomes by Donaldson, R.P, Fang, T.K

“…Glyoxysomes isolated from castor bean (Ricinus communis L., var Hale) endosperm had NADH:ferricyanide reductase and NADH:cytochrome c reductase activities…”
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Wavelength dependence of the nonresonant photoionization cross section of a two-electron atom near the ionization threshold by Chang, TN, Fang, TK

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Regulation of the phosphorylation of mitochondrial pyruvate dehydrogenase complex in situ. Effects of respiratory substrates and calcium by Budde, R.J.A, Fang, T.K, Randall, D.D

“…The activity of the pyruvate dehydrogenase complex (PDC), as controlled by reversible phosphorylation, was studied in situ with mitochondria oxidizing…”
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