Quantitative cytochemical localization of cinnamyl alcohol dehydrogenase activity in plant tissues

1993 ◽  
Vol 4 (5) ◽  
pp. 205-209 ◽  
Author(s):  
S. Baudracco ◽  
J. Grima-Pettanati ◽  
A. M. Boudet ◽  
P. B. Gahan
1973 ◽  
Vol 19 (3) ◽  
pp. 353-358 ◽  
Author(s):  
Casimir J. Woscinski ◽  
Dan O. McClary

Whole-cell extracts of Rhodotorula glutinis grown on yeast extract – glucose medium contained minute quantities of NAD-dependent alcohol dehydrogenase and cinnamyl alcohol dehydrogenase. Significantly greater quantities of these enzymes, as well as an NADP-dependent alcohol dehydrogenase were contained by cells grown on the same medium with ethanol substituted for glucose as the growth substrate. Although the [Formula: see text] on ethanol of whole cells grown in ethanol medium was more than triple that of cells grown in glucose medium, there was no significant difference in the [Formula: see text] on glucose of whole cells grown in glucose or in ethanol medium. Thermal inactivation studies revealed that the NADP-dependent alcohol dehydrogenase was relatively heat-stable as compared with the NAD-dependent alcohol dehydrogenase. Gel column electrophoresis revealed three active bands of alcohol dehydrogenase activity which were identified as NAD-dependent alcohol dehydrogenase, NADP-dependent alcohol dehydrogenase, and cinnamyl alcohol dehydrogenase. The NAD- and NADP-dependent enzymes, particularly the latter, were active on higher alcohols but not on methanol.


Tsitologiya ◽  
2018 ◽  
Vol 60 (6) ◽  
pp. 469-475
Author(s):  
O. D. Nimaeva ◽  
◽  
E. V. Pradedova ◽  
A. B. Karpova ◽  
R. K. Salyaev ◽  
...  

1998 ◽  
Vol 49 (2) ◽  
pp. 295-306 ◽  
Author(s):  
Nabila Yahiaoui, Christiane Marque ◽  
Hélène Corbière ◽  
Alain Michel Boudet

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