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Maize, alcohol dehydrogenase

Sachs, M.M., Dennis, E.S., Gerlach, W.L. Peacock, W.J. (1986). Two alleles of maize alcohol dehydrogenase I have 3 structural and poly(A) addition polymorphisms. Genetics, 113, 449-67. [Pg.179]

J. C. Walker, E. A. Howard, E. S. Dennis, W. J. Peacock (1987) DNA sequences required for anaerobic expression of the maize alcohol dehydrogenase I gene. Proc. Natl. Acad. Sci. USA, 84 6624-6628... [Pg.127]

Fig. 3. Protein synthesis in a maize primary root during ( ) one hr pulse labelling with [ HJleucine under aerobic conditions (b)-(e) pulse labelling with [ HJIeucine during the specified times under anaerobic conditions. The arrow labelled TPs indicates the position of the transition polypeptides. The unlabelled arrow indicates the position of alcohol dehydrogenase 1 (ADHl). From Sachs et al. (1980). Fig. 3. Protein synthesis in a maize primary root during ( ) one hr pulse labelling with [ HJleucine under aerobic conditions (b)-(e) pulse labelling with [ HJIeucine during the specified times under anaerobic conditions. The arrow labelled TPs indicates the position of the transition polypeptides. The unlabelled arrow indicates the position of alcohol dehydrogenase 1 (ADHl). From Sachs et al. (1980).
Hake, S., Kelley, P.M., Taylor, W.C. Freeling, M. (1985). Coordinate induction of alcohol dehydrogenase 1, aldolase, and other anaerobic RNAs in maize. Journal of Biological Chemistry, 260, 5050-4. [Pg.176]

Sachs, M.M. Freeling, M. (1978). Selective synthesis of alcohol dehydrogenase during anaerobictreatment of maize. Mo/ecw/ar andCcMera/Ccncrics, 161,111-15. [Pg.179]

Halpin, C., Holt, K., Chojecki, J., Oliver, D., Chabbert, B., Monties, B., Edwards, K., Barakate, A., and Foxon, G. A., 1998, Brown-midrib maize (bml) - a mutation affecting the cinnamyl alcohol dehydrogenase gene, Plant J. 14 545-553. [Pg.139]

Walter, M.H., Grima-Pettenati, J., Grand, C., Boudet, A.M. Lamb, C.J. (1990). Extensive sequence similarity of the bean CAD4 (cin-namyl-alcohol dehydrogenase) to a maize malic enzyme. Plant Molecular Biology 15, 525-6. [Pg.111]

Fig. 7. Diagrams of the schemes for modifying levels of A, alcohol dehydrogenase and B, pyruvate decarboxylase activity and testing for survival of anoxia. In A, constructs contain the 35S promoter of the cauliflower mosaic virus (35S) driving expression of the cotton Adh cDNA in either the sense (Adh) or antisense (hdA) orientation, linked to the 3 termination signal of the nopaline synthase gene (Nos). Alternatively, the expression of cotton Adh cDNA is under control of the pea Adh promoter sequence (pea Adh). In B, either the 35S promoter or the pea Adh promoter is used to drive expression of the maize pyruvate decarboxylase cDNA (Pdc), linked to a Nos 3 termination sequence. Constructs are introduced into cotton via Agrobacterium tumefaciens-mediated infection of cotton. Transformed cotton callus is then assayed for its ability to survive anoxia. Fig. 7. Diagrams of the schemes for modifying levels of A, alcohol dehydrogenase and B, pyruvate decarboxylase activity and testing for survival of anoxia. In A, constructs contain the 35S promoter of the cauliflower mosaic virus (35S) driving expression of the cotton Adh cDNA in either the sense (Adh) or antisense (hdA) orientation, linked to the 3 termination signal of the nopaline synthase gene (Nos). Alternatively, the expression of cotton Adh cDNA is under control of the pea Adh promoter sequence (pea Adh). In B, either the 35S promoter or the pea Adh promoter is used to drive expression of the maize pyruvate decarboxylase cDNA (Pdc), linked to a Nos 3 termination sequence. Constructs are introduced into cotton via Agrobacterium tumefaciens-mediated infection of cotton. Transformed cotton callus is then assayed for its ability to survive anoxia.
Howard, E.A., Walker, J.C., Dennis, E.S. Peacock, W.J. (1987). Regulated expression of an alcohol dehydrogenase-1 chimeric gene introduced into maize protoplasts. Planta 170, 535-40. [Pg.244]

Maize Adhl Alcohol dehydrogenase Christie etal., 1991... [Pg.277]

Christie, P.J., Hahn, M. Walbot, W. (1991). Low temperature accumulation of alcohol dehydrogenase-1 mRNA and protein activity in maize and rice seedlings. Plant Physiology 95, 699-706. [Pg.284]

Pyruvate decarboxylase (EC 4.1.1.1) has been characterized in different sources including yeast, bacteria, wheat, maize, sweet potato, and plants [8]. This is the first enzyme of the branch of the glycolytic pathway, which under anaerobic conditions leads to nonoxidative decarboxylation of pyruvate to reduced end-products [9]. In the case of yeast, pyruvate decarboxylase together with alcohol dehydrogenase (EC 1.1.1.1) converts pyruvate to ethanol. [Pg.268]


See other pages where Maize, alcohol dehydrogenase is mentioned: [Pg.176]    [Pg.176]    [Pg.166]    [Pg.168]    [Pg.175]    [Pg.123]    [Pg.231]    [Pg.243]    [Pg.274]    [Pg.164]    [Pg.411]    [Pg.74]    [Pg.98]    [Pg.627]    [Pg.223]    [Pg.23]    [Pg.328]    [Pg.514]    [Pg.514]   
See also in sourсe #XX -- [ Pg.188 ]




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