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Whole genome sequencing-based multi-locus association mapping for kernel iron, zinc and protein content in groundnut. [PDF]
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Induction of threonine dehydratase in foetal rat liver
Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 1973Abstract 1. 1. Administration of glucose to newborn rats at the time of delivery results in significant repression of the development of hepatic threonine dehydratase activity. 2. 2. Injection of insulin to pregnant rats leads to precocious appearance of hepatic threonine dehydratase activity in foetal rats. 3. 3.
D Yeung
exaly +3 more sources
Hormonal induction of threonine dehydratase in postnatal rat liver
Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 1974Abstract 1. 1. Insulin administration to neonatal rats results in either potentiation or repression of the development of hepatic threonine dehydratase according to the dosage employed. 2. 2. Simultaneous injections of glucagon and adrenaline to newborn rats do not elicit a greater inductive effect than administration of each hormone alone.
Y G, Yeung, D C, Yeung
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The postnatal induction of threonine dehydratase in rat liver
International Journal of Biochemistry & Cell Biology, 19721. 1. Administration of actinomycin D or cyclohcximide to rats at the time of surgical delivery results in complete repression of the development of threonine dehydratase activity. 2. 2. Precocious development of the enzyme may be brought about by injection of glucagon or adrenaline to foetal rats in utero. 3. 3.
D Yeung
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Threonine dehydratase from goat liver
Archives of Biochemistry and Biophysics, 1972Abstract Threonine dehydratase has been purified 374-fold from extracts of goat liver by controlled heat treatment, ammonium sulfate fractionation and DEAE-cellulose column chromatography. The optimum activity was found between pH 8.0–9.0. The temperature optimum was 70 °C under the conditions of assay. The enzyme was inhibited by pyridoxal phosphate
M, Nath, G G, Sanwal
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Double inhibition ofl-threonine dehydratase by aminothiols
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1989The inhibition of highly purified rat liver L-threonine dehydratase (L-threonine hydro-lyase (deaminating), EC 4.2.1.16) by aminothiols (L-cysteine, D-cysteine, cysteamine) has been studied. Single inhibition experiments evaluated by Lineweaver-Burk and Dixon plots showed, in a given concentration range, partially (parabolic) competitive inhibitions ...
LEONCINI, ROBERTO +3 more
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The Journal of Nutrition, 1978
The metabolic fate of threonine was investigated in young male rats fed 15% amino acid diets containing from 0.15% to 0.85% of L-threonine. Liver serine-threonine dehydratase (S-TDH) activity did not increase with increasing dietary threonine content.
Y A, Kang-Lee, A E, Harper
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The metabolic fate of threonine was investigated in young male rats fed 15% amino acid diets containing from 0.15% to 0.85% of L-threonine. Liver serine-threonine dehydratase (S-TDH) activity did not increase with increasing dietary threonine content.
Y A, Kang-Lee, A E, Harper
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Threonine dehydratases in different strains of Streptomyces fradiae
Journal of Biotechnology, 1995Among Streptomyces fradiae parent strain (NRRL 2702), aspartate auxotroph strain (SMF 305), and revertant strain (SMF 306), the revertant strain is the highest producer of tylosin and showed different repression patterns of tylosin production by ammonium ion from the parent strain.
S H, Lee, K J, Lee
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The threonine dehydratase structural gene in Aspergillus nidulans
Biochimica et Biophysica Acta (BBA) - General Subjects, 1974Abstract Mutations at the ile A locus of Aspergillus nidulans can lead to loss of threonine dehydratase ( l -threonine hydro-lyase (deaminating), EC 4.2.1.16), the first enzyme for isoleucine biosynthesis. A cold-sensitive allele, ile A-13, leads to production of an enzyme having an increased apparent K m for l -threonine and showing ...
D W, MacDonald, H N, Arst, D J, Cove
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A spectrophotometric method for the assay of threonine dehydratase
Analytical Biochemistry, 1965Abstract The enzymic conversion of β-hydroxy α-amino acids to α-keto acids by ThrDH (sheep liver) was followed by a direct spectrophotometric method at 230 mμ. The assay was more sensitive to changes in keto acid concentrations than the 2,4-dinitrophenylhydrazone method because of the absence of the high and variable blanks of the latter method ...
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