Search Results - "SUNDARAM, T. K"

Catalytic-rate improvement of a thermostable malate dehydrogenase by a subtle alteration in cofactor binding by Alldread, R M, Halsall, D M, Clarke, A R, Sundaram, T K, Atkinson, T, Scawen, M D, Nicholls, D J

“…The nucleotide-binding fold of many NAD(+)-dependent dehydrogenases contains a conserved acidic amino acid residue which hydrogen-bonds with the 2'- and…”
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Regulation of isocitrate dehydrogenase by phosphorylation in Escherichia coli K-12 and a simple method for determining the amount of inactive phosphoenzyme by EDLIN, J. D, SUNDARAM, T. K

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Malate dehydrogenases from actinomycetes: structural comparison of Thermoactinomyces enzyme with other actinomycete and Bacillus enzymes by SMITH, K, SUNDARAM, T. K, KERNICK, M

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Malate dehydrogenase from thermophilic and mesophilic bacteria. Molecular size, subunit structure, amino acid composition, immunochemical homology, and catalytic activity by Sundaram, T. K, Wright, I. P, Wilkinson, A. E

“…Malate dehydrogenases isolated from a number of mesophilic, moderately thermophilic, and extremely thermophilic bacteria yield upon denaturation subunits of…”
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Overexpression of the Thermus aquaticus B malate dehydrogenase-encoding gene in Escherichia coli by Alldread, R M, Nicholls, D J, Sundaram, T K, Scawen, M D, Atkinson, T

“…Expression of the Thermus aquaticus B malate dehydrogenase (MDH)-encoding gene (mdh), cloned in Escherichia coli, was initially at a relatively low level (0.1%…”
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Isolation and characterization of isocitrate lyase from a thermophilic Bacillus sp by Chell, R M, Sundaram, T K, Wilkinson, A E

“…Isocitrate lyase was isolated in homogeneous state from a thermophilic Bacillus. The enzyme has a mol.wt. of 180000 and a pI of 4.5 and contains threonine as…”
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Physiological Role of Pyruvate Carboxylase in a Thermophilic Bacillus by Sundaram, T K

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Action of surfactants on porcine heart malate dehydrogenase isoenzymes and a simple method for the differential assay of these isoenzymes by Smith, K, Sundaram, T K

“…The cationic surfactant, cetyl (hexadecyl) trimethylammonium bromide (CTAB), completely inactivates porcine heart cytoplasmic malate dehydrogenase…”
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Cloning sequencing and over-expression of Escherichia coli malate dehydrogenase by NICHOLLS, D. J, MINTON, N. P, ATKINSON, T, SUNDARAM, T. K

“…The malate dehydrogenase gene (mdh ) from E. coli W3899 has been cloned and its nucleotide sequence determined. A comparison of the DNA sequence presented here…”
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Regulation of myo-Inositol Catabolism in Aerobacter aerogenes by Sundaram, T K

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Structural basis of the thermostability of monomeric malate synthase from a thermophilic Bacillus by Chell, R M, Sundaram, T K

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Nucleotide sequence of the succinyl-CoA synthetase alpha-subunit from Thermus aquaticus B by NICHOLLS, D. J, SUNDARAM, T. K, ATKINSON, T, MINTON, N. P

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Energetics of Bacillus stearothermophilus growth: molar growth yield and temperature effects on growth efficiency by Coultate, T P, Sundaram, T K

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Isocitrate Lyase from a Thermophilic Bacillus: Effect of Salts on Enzyme Activity by Griffiths, M W, Sundaram, T K

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Pyruvate carboxylase from a thermophilic bacillus: some molecular characteristics by Libor, Susan, Sundaram, T. K, Warwick, Rita, Chapman, J. A, Grundy, S. M. W

“…Analysis of the native enzyme and of the subunits produced upon its denaturation shows that pyruvate carboxylase from a thermophilic Bacillus is a tetramer…”
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Stability and immunological cross-reactivity of malate dehydrogenases from mesophilic and thermophilic sources by Smith, K, Sundaram, T K

“…The thermostability in vitro of dimeric and tetrameric malate dehydrogenases [S)-malate:NAD+ oxidoreductase, EC 1.1.1.37) from mesophilic and thermophilic…”
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Simple efficient methods for the isolation of malate dehydrogenase from thermophilic and mesophilic bacteria by Wright, I P, Sundaram, T K

“…Malate dehydrogenase from a number of bacteria drawn from several genera and representing the mesophilic, moderately thermophilic and extremely thermophilic…”
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Regulation of Pyruvate Carboxylase Formation from the Apo-enzyme and Biotin in a Thermophilic Bacillus by CAZZULO, J. J, SUNDARAM, T. K, KORNBERG, H. L

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Benign chondroblastoma by Sundaram, T K

“…1. Benign chondroblastoma is a rare primary neoplasm of bone with excellent prognosis. It is believed that instances of it are still being missed. 2. Six cases…”
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Mechanism of Pyruvate Carboxylase Formation from the Apo-Enzyme and Biotin in a Thermophilic Bacillus by CAZZULO, J. J, SUNDARAM, T. K, KORNBERG, H. L

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