scholarly journals Molecular analysis of the alcohol dehydrogenase 2 (Adh2) gene of maize

1985 ◽  
Vol 13 (3) ◽  
pp. 727-743 ◽  
Author(s):  
E.S. Dennis ◽  
M.M. Sachs ◽  
W.L. Gerlach ◽  
E.J. Finnegan ◽  
W.J. Peacock
2005 ◽  
Vol 274 (4) ◽  
pp. 354-363 ◽  
Author(s):  
R. A. Rangel-Porras ◽  
V. Meza-Carmen ◽  
G. Martinez-Cadena ◽  
J. C. Torres-Guzmán ◽  
G. A. González-Hernández ◽  
...  

1988 ◽  
Vol 150 (2) ◽  
pp. 655-664 ◽  
Author(s):  
Mark A. Batzer ◽  
Trent D. Desselle ◽  
Mark D. Brennan ◽  
William R. Lee ◽  
Bruce Tedeschi

2000 ◽  
Vol 15 (2) ◽  
pp. 97-102 ◽  
Author(s):  
S. Amadéo ◽  
E.P. Noble ◽  
M.L. Fourcade-Amadéo ◽  
C. Tetaria ◽  
M.F. Brugiroux ◽  
...  

SummaryAlleles of the D2 dopamine receptor (DRD2) and the alcohol dehydrogenase 2 (ADH2) genes were determined in 69 French Polynesian alcoholic patients and 57 controls matched for racial origin. Three racial groups were studied: pure Polynesians (PP), Polynesians mixed with Caucasian (PCA) ancestry and Polynesians mixed with Chinese (PCH) ancestry. DRD2 A1 allele frequencies in the alcoholics compared to their controls in these groups were: PP,.26 vs .32 (P = .69); PCA, .44 vs .35 (P = .46); PCH, .40 vs 0.39 (P = .88). ADH2 1 allele frequencies in alcoholics compared to their controls groups were: PP, .56 vs .62 (P = .66); PCA, .75 vs .56 (P = .09); PCH, .78 vs .32 (P = .009). In the PCA group, the combination of the DRD2 A1 genotypes and the ADH2 1 homozygotes was strongly associated with alcoholism (P = .0027). This preliminary study shows the importance of ascertaining racial ancestry in molecular genetic association studies. Moreover, it suggests that a combination of genes are involved in susceptibility to the development of alcoholism.


1995 ◽  
Vol 310 (3) ◽  
pp. 983-988 ◽  
Author(s):  
E K Mutenda ◽  
M J Sparkes ◽  
H B F Dixon

The isosteric arsenical analogue of glycerol 3-phosphate, 3,4-dihydroxybutylarsonic acid, is a good substrate for rabbit muscle glycerol-3-phosphate dehydrogenase. Its oxidation is accompanied by release of arsenite. This release seems to be due to a spontaneous elimination of arsenite by 3-oxoalkylarsonic acids, as it is also observed in (1) the oxidation of 3-hydroxypropylarsonic acid by yeast alcohol dehydrogenase, (2) treatment of 3,4-dihydroxybutylarsonic acid with periodate and (3) nonenzymic transamination of the glutamate analogue 2-amino-4-arsonobutyric acid. Enzymic formation of 3-oxoalkylarsonic acids in cells can therefore be lethal, as arsenite is poisonous to most organisms because of its high affinity for dithiols such as dihydrolipoyl groups.


1984 ◽  
Vol 12 (9) ◽  
pp. 3983-4000 ◽  
Author(s):  
E.S. Dennis ◽  
W.L. Gerlach ◽  
A.J. Pryor ◽  
J.L. Bennetzen ◽  
A. Inglis ◽  
...  

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