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Alcohol dehydrogenase inactivator from rice seedlings: properties and intracellular location

Journal Article · · Plant Physiol.; (United States)
DOI:https://doi.org/10.1104/pp.71.4.742· OSTI ID:6271268
The alcohol dehydrogenase (ADH) inactivator from aerobically grown rice (Oryza sativa) coleoptiles was shown to be associated with membranes which were recovered in sucrose gradients at peak density 1.13 grams per cubic centimeter. When Mg/sup 2 +/ was included in the gradient, the inactivator was recovered at peak density 1.16 grams per cubic centimeter coinciding with the marker enzyme for endoplasmic reticulum, antimycin A-insensitive NADH cytochrome c reductase. ADH was recovered exclusively in cytosol fractions. The inactivator attacks ADH from several plant sources and from yeast. There was no evidence for proteolysis when pure yeast ADH was inactivated by the inactivator, but there was a loss of SH groups from ADH during inactivation which was restored after incubation with dithiothreitol under denaturing conditions. The inactivator did not attach other SH enzymes tested but did result in loss of SH groups from glutathione and dithiothreitol which prevent ADH inactivation. When O/sub 2/ was removed from the inactivator assay medium, the inactivation as well as the loss of SH groups from yeast ADH was significantly depressed.
Research Organization:
Univ. of California, Santa Cruz
DOE Contract Number:
AC03-76SF00098
OSTI ID:
6271268
Journal Information:
Plant Physiol.; (United States), Journal Name: Plant Physiol.; (United States) Vol. 71; ISSN PLPHA
Country of Publication:
United States
Language:
English

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