Isolation of alcohol dehydrogenases from germinating seeds of pea, broad-bean, lentil and kidney-bean
Author:
Publisher
Institute of Experimental Botany
Subject
Horticulture,Plant Science
Link
http://link.springer.com/content/pdf/10.1007/BF02922760
Reference29 articles.
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3. Coleman, P. L., Iweibo, I., Weiner, H.: Role of zinc in horse liver ADH. — Influence on structure and conformation changes. — Biochemistry11: 1010–1016, 1972.
4. Cossins, E. A., Kopala, L. C., Blowacky, B., Spnonk, A. M.: Some properties of higher plant alcohol dehydrogenase. — Phytochemistry7: 1125–1134, 1968.
5. Cossins, E. A., Turner, E. R.: Losses of alcohol and alcohol dehydrogenasc activity in germinating seeds. — Ann. Bot.26: 591–597, 1962.
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1. Effect of sprouting on the proteome of chickpea flour and on its digestibility by ex vivo gastro-duodenal digestion complemented with jejunal brush border membrane enzymes;Food Research International;2022-04
2. The variations in isoenzyme patterns of alcohol dehydrogenase and their substrate specificity in germinating pea seeds;Biologia Plantarum;1981-05
3. Pea alcohol dehydrogenase: Substrate specificity and binding of coenzyme to enzyme;Collection of Czechoslovak Chemical Communications;1979
4. The reduction of aldehydes by broad bean and maize alcohol dehydrogenases and a study of the substrate binding to the enzyme protein;Biologia Plantarum;1978-05
5. Dormancy in Seeds;Annual Review of Plant Physiology;1977-06
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