Results 271 to 280 of about 561,527 (291)
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"Galactose Dehydrogenase," "Nothing Dehydrogenase," and Alcohol Dehydrogenase: Interrelation
Science, 1967Stanton Segal, Pedro Cuatrecasas
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Alcohol dehydrogenases and aldehyde dehydrogenases
Biochemical Society Transactions, 1988Hans Jörnvall+6 more
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1980
In 196 Michael Rossmann, Herman Watson and Carl Branden in the Cambridge laboratory of Max Perutz and John Kendrew occasionally discussed future crystallographic projects which might illuminate structure — function relationships within families of proteins.
Hans Eklund, Carl-Ivar Brändén
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In 196 Michael Rossmann, Herman Watson and Carl Branden in the Cambridge laboratory of Max Perutz and John Kendrew occasionally discussed future crystallographic projects which might illuminate structure — function relationships within families of proteins.
Hans Eklund, Carl-Ivar Brändén
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LACTIC DEHYDROGENASE AND SUCCINIC DEHYDROGENASE IN PSORIASIS
British Journal of Dermatology, 1967I. Belšan+2 more
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Glyoxylate Dehydrogenase Activity of Lactate Dehydrogenase*
The Journal of Biochemistry, 1967Shunji Sawaki+2 more
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Asparate dehydrogenase activity of malate dehydrogenase
Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects, 1964Charles R. Shaw, Ann L. Koen
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[35] Asparagusate dehydrogenase and lipoyl dehydrogenase from asparagus
1979Publisher Summary Asparagusate dehydrogenase and lipoyl dehydrogenase are essential components of asparagus pyruvate dehydrogenase complexes, which catalyze a CoA- and NAD-linked oxidative decarboxylation of pyruvate. These two enzymes are flavoproteins and catalyze the oxidoreduction of asparagusate and lipoate. Asparagusate dehydrogenase and lipoyl
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Effects of Cyanamide on Alcohol Dehydrogenase and Aldehyde Dehydrogenase
The Journal of Biochemistry, 1961Haruhiko Ando, Ichiro Fuwa
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Molybdenum-containing CO dehydrogenase and formate dehydrogenases
The molybdenum-containing CO dehydrogenase and the formate dehydrogenases catalyze important interconversions of one-carbon compounds, the former oxidizing CO to CO2, and the latter the reversible interconversion of CO2 and formate. Methodologies to study these two enzymes are discussed.openaire +2 more sources