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l threonine/maïs
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Changes in Enzyme Regulation during Growth of Maize: I. Progressive Desensitization of Homoserine Dehydrogenase during Seedling Growth.
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The sensitivity of homoserine dehydrogenase (EC 1.1.1.3) to inhibition by the feed-back modifier, l-threonine, was examined in preparations derived from etiolated shoots, roots, and lightgrown tissues of Zea mays L. var. earliking. A progressive decrease in enzyme sensitivity was observed during
Changes in Enzyme Regulation during Growth of Maize: II. Relationships among Multiple Molecular Forms of Homoserine Dehydrogenase.
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The relative contribution of each of several forms of homoserine dehydrogenase (EC 1.1.1.3) to the total enzyme population in etiolated shoots and in roots of Zea mays L. var. earliking was examined by the use of gel filtration chromatography and disc gel electrophoresis. In enzyme preparations
Ligand-induced interconversions of maize homoserine dehydrogenase among different states.
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The threonine-sensitive homoserine dehydrogenase has been isolated and extensively purified from shoots of Zea mays L. var. earliking. This enzyme is shown to be hysteretic under certain conditions. Progress curves of the NAD-dependent reaction catalyzed by the maize enzyme can be characterized by
Differential Regulation of Maize Homoserine Dehydrogenase under Physiological Conditions.
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Homoserine dehydrogenase is associated with the multibranched pathway of amino acid biosynthesis originating with aspartic acid. Like most of the related pathway enzymes, this enzyme is localized in chloroplasts. The activity and regulatory properties of the threonine-sensitive isozyme of homoserine
Tissue culture isolation of a second mutant locus for increased threonine accumulation in maize.
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Regenerable maize (Zea mays L.) tissue cultures were selected for ability to grow in the presence of inhibitory (1.0-1.5 mM) concentrations of L-lysine plus L-threonine. Testcross kernels from one regenerated plant (LT20) segregated for wild-type and high free threonine concentration in a 1∶1 ratio
Genetic and amino-acid analysis of two maize threonine-overproducing, lysine-insensitive aspartate kinase mutants.
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The aspartate-derived amino-acid pathway leads to the production of the essential amino-acids lysine, methionine, threonine and isoleucine. Aspartate kinase (AK) is the first enzyme in this pathway and exists in isoforms that are feedback inhibited by lysine and threonine. Two maize (Zea mays L.)
Effects of plant age and extraction conditions on the properties of homoserine dehydrogenase isolated from maize seedlings.
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Homoserine dehydrogenase (EC 1.1.1.3) was extracted from shoots of etiolated seedlings of Zea mays L. which had been grown for periods ranging from three to thirteen days. Both the amount of enzyme extracted and its regulatory properties, as measured by the sensitivity of the enzyme to inhibition by
Changes in Enzyme Regulation during Growth of Maize: III. Intracellular Localization of Homoserine Dehydrogenase in Chloroplasts.
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Extracts of leaf tissue of Zea mays L. seedlings were fractionated on nonlinear sucrose gradients to separate subcellular organelles. Homoserine dehydrogenase (EC 1.1.1.3) was identified in those fractions containing intact chloroplasts, as judged by the presence of chlorophyll and triosephosphate
Comparison of sensitive and desensitized forms of maize homoserine dehydrogenase.
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The properties of homoserine dehydrogenase (EC 1.1.1.3) isolated from shoots of young etiolated seedlings of Zea mays L. var. earliking can be reversibly altered by dialysis against an appropriate buffer. Treatment with 500 millimolar potassium phosphate buffer (pH 7.5) in the absence of l-threonine
Dietary protein restriction and fat supplementation diminish the acidogenic effect of exercise during repeated sprints in horses.
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A restricted protein diet supplemented with amino acids and fat may reduce the acidogenic effects of exercise. Twelve Arabian horses were assigned to a 2 x 2 factorial experiment: two fat levels: 0 or 10 g/100 g added corn oil and two crude protein levels: 7.5 g/100 g (supplemented with 0.5%
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