Reptilian alcohol dehydrogenase: Isozyme divergence among submammalian vertebrates

1992 ◽  
Vol 11 (4) ◽  
pp. 412-412
Author(s):  
Lars Hjelmqvist ◽  
Jawed Shafqat ◽  
Hans Jörnvall
Keyword(s):  
Alcohol Dehydrogenase ◽  
Dehydrogenase Isozyme

Cloning and Expression of a Human Stomach Alcohol Dehydrogenase Isozyme

1995 ◽  
pp. 341-347 ◽  
Author(s):  
Natalia Y. Kedishvili ◽  
William F. Bosron ◽  
Carol L. Stone ◽  
Cara F. Peggs ◽  
Holly R. Thomasson ◽  
...  
Keyword(s):  
Alcohol Dehydrogenase ◽  
Human Stomach ◽  
Cloning And Expression ◽  
Dehydrogenase Isozyme

Physical and enzymic properties of a class II alcohol dehydrogenase isozyme of human liver: .pi.-ADH

Biochemistry ◽  
1984 ◽  
Vol 23 (26) ◽  
pp. 6363-6368 ◽  
Author(s):  
Charles C. Ditlow ◽  
Barton Holmquist ◽  
Maurice M. Morelock ◽  
Bert L. Vallee
Keyword(s):  
Alcohol Dehydrogenase ◽  
Human Liver ◽  
Class Ii ◽  
Dehydrogenase Isozyme

The Control of Alcohol Dehydrogenase Isozyme Synthesis in Saccharomyces cerevisiae

1972 ◽  
Vol 50 (1) ◽  
pp. 35-43 ◽  
Author(s):  
P. Wendy Fowler ◽  
Alan J. S. Ball ◽  
David E. Griffiths
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Alcohol Dehydrogenase ◽  
Catabolite Repression ◽  
Isozyme Pattern ◽  
Isolated Mitochondria ◽  
Mechanical Disruption ◽  
Dehydrogenase Isozyme

Isozymes of alcohol dehydrogenase (ADH) from yeast were separated by discontinuous electrophoresis. Three major bands were observed: ADH-I, ADH-II, and a new band designated mito-ADH. Work with isolated mitochondria showed that the mito-ADH band could be produced from physiologically competent mitochondria by mechanical disruption or by treatment with detergents.The isozyme pattern was determined for the various physiological states of yeast growing anaerobically and aerobically on 2% glucose and aerobically on 2% ethanol, and for catabolite de-repressed cells undergoing an anaerobic → aerobic transition in continuous culture.The changing isozyme pattern substantiates the thesis that ADH-I is produced constitutively and that ADH-II is regulated via catabolite repression. It appears from the data that mito-ADH is more closely related to mitochondriogenesis than is ADH-II.

Purification and kinetic characterization of pickerel liver alcohol dehydrogenase with dual coenzyme specificity

1993 ◽  
Vol 71 (9-10) ◽  
pp. 421-426 ◽  
Author(s):  
Loola S. Al-Kassim ◽  
C. Stan Tsai
Keyword(s):  
Alcohol Dehydrogenase ◽  
Gel Filtration ◽  
Kinetic Studies ◽  
Resonance Spectroscopy ◽  
Coenzyme Specificity ◽  
Liver Alcohol Dehydrogenase ◽  
Steady State Kinetic ◽  
Dehydrogenase Isozyme ◽  
State Kinetic

A major alcohol dehydrogenase isozyme that displays dual coenzyme specificity has been purified from pickerel liver by ion-exchange, gel filtration, and affinity chromatographic procedures. The purified enzyme is chromatographically and electrophoretically homogeneous. It is dimeric and possesses common physical properties shared by other liver alcohol dehydrogenases. Phosphorus-31 nuclear magnetic resonance spectroscopy demonstrates that NADP+ binds to two coenzyme sites of the pickerel enzyme. Steady-state kinetic studies suggest that pickerel liver alcohol dehydrogenase catalyzes NAD(P)+-linked ethanol oxidation via a random pathway. While the NADP+ reduction involves the formation of an abortive complex at high NADP+ concentrations, the NAD+ reduction at low NAD+ concentrations follows an ordered Bi-Bi mechanism with NAD+ being the leading reactant.Key words: purification, pickerel liver, alcohol dehydrogenase.

scholarly journals Purification and Properties of an Alcohol Dehydrogenase Isozyme from a Methanol-using Yeast, Candida sp. N-16

1992 ◽  
Vol 56 (2) ◽  
pp. 338-339 ◽  
Author(s):  
Motoaki Yabe ◽  
Kazuyuki Shitara ◽  
Jun Kawashima ◽  
Hirofumi Shinoyama ◽  
Akikazu Ando ◽  
...  
Keyword(s):  
Alcohol Dehydrogenase ◽  
Candida Sp ◽  
Purification And Properties ◽  
Dehydrogenase Isozyme
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