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The Proton-translocating NADH-Quinone Oxidoreductase (NDH-1) of Thermophilic Bacterium Thermus thermophilus HB-8
The genes encoding the proton-translocating NADH-quinone oxidoreductase (NDH-1) of a thermophilic bacterium Thermus thermophilus HB-8 were cloned and sequenced, and results strongly suggest that the T. thermphilus NDH-2 subunit is similar to other NDh-1 enzyme complexes in terms of subunit and cofactor composition.
pH dependence of the hydrolysis of hippuric acid esters by carboxypeptidase A.
The pH dependence (pH 4.5-10.5) of the hydrolysis of seven hippuric acid esters by bovine carboxypeptidase A has been investigated, and the pH dependence of the substrate activation of 1a-c and the substrate inhibition of 1d-g have been compared.
Substrate inhibition in the hydrolysis of N-acylglycine esters by carboxypeptidase A.
Data is available which can only be interpreted in terms of at least three enzymic sites being available for hydrophobic interactions with ester substrate molecules.
Detection by low temperature spectrophotometry of a mixed anhydride intermediate in the carboxylate ion-catalysed hydrolysis of a sulphite ester
By low temperature spectrophotometry in aqueous ethylene glycol solutions we have observed two phases corresponding to the release of p-nitrophenol in both stages of the chloroacetate ion-catalysed
Further studies of the specificity of carboxypeptidase A towards hippuric acid esters
The kinetics of hydrolysis of a series of 10 new hippurate esters (C6H5CONHCH2CO2CRR1CO2H (I)) by bovine pancreatic carboxypeptidase A have been investigated at pH 7.5, 25 °C, and ionic strength 0.5.
A simple sub-zero trap for moisture removal
  • S. S. Chu
  • Environmental Science
  • 1 February 1979