• Publications
  • Influence
Studies on reactions of illuminated chloroplasts. I. Mechanism of the reduction of oxygen and other Hill reagents.
  • A. Mehler
  • Chemistry, Medicine
  • Archives of biochemistry and biophysics
  • 1 August 1951
Abstract 1. 1. The evolution of oxygen by illuminated chloroplasts does not involve the intermediate production of H 2 O 2 in a form available to the enzyme catalase. 2. 2. Illuminated chloroplastsExpand
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The enzymatic mechanism of oxidation-reductions between malate or isocitrate and pyruvate.
The discovery of carbon dioxide assimilation by heterotrophic bacteria (1) and animal tissues (2) aroused considerable interest in the mechanisms involved. Evidence from various sources suggested theExpand
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Studies on reactions of illuminated chloroplasts. II. Stimulation and inhibition of the reaction with molecular oxygen.
  • A. Mehler
  • Chemistry, Medicine
  • Archives of biochemistry and biophysics
  • 1 December 1951
Abstract 1. 1. The consumption of oxygen by illuminated chloroplasts in the presence of catalase and ethanol reported earlier is shown to be stimulated by prior Hill reaction with quinone. ThisExpand
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Studies on oxygenases; enzymatic formation of kynurenine from tryptophan.
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Deamination of histidine to form urocanic acid in liver.
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The conversion of tryptophan to kynurenine in liver. I. The coupled tryptophan peroxidase-oxidase system forming formylkynurenine.
  • W. Knox, A. Mehler
  • Biology, Medicine
  • The Journal of biological chemistry
  • 1 November 1950
The enzyme reactions bringing about oxidation in the indole ring of tryptophan and kynurenine formation furnish a convenient example of those poorly understood systems producing aromatic ringExpand
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The adaptive increase of the tryptophan peroxidase-oxidase system of liver.
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MECHANISM OF THE ALDOLASE REACTION.
Upon treatment with carboxypeptidase, muscle aldolase (ketose-l-phosphate aldehyde-lyase, EC 4.1.2.7) loses 3 COOHterminal tyrosine residues (3, 4) and exhibits a 20-fold fall in the rate of fructoseExpand
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