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PLANT PHYSIOLOGY , Vol 102, Issue 3 867-872, Copyright © 1993 by American Society of Plant Biologists
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DEVELOPMENT AND GROWTH REGULATION |
Partial Purification of a cis-trans-Isomerase of Zeatin from Immature Seed of Phaseolus vulgaris L
N. V. Bassil, DWS. Mok and M. C. Mok
Department of Horticulture and Center for Gene Research and Biotechnology, Oregon State University, Corvallis, Oregon 97331
Investigation of the conversion of exogenous cis-zeatin to trans-zeatin in
immature seeds of Phaseolus vulgaris L. led to the isolation of a
cis-trans-isomerase from the endosperm. The enzyme was purified more than
2000-fold by chromatography on a series of fast protein liquid
chromatography (anion exchange, gel filtration, and hydrophobic
interaction) and concanavalin A columns. The enzymic reaction favors
conversion from the cis to the trans form and requires flavin, light, and
dithiothreitol. cis-Zeatin riboside is also a substrate for the enzyme.
Retention on the concanavalin A column indicated that the enzyme is a
glycoprotein. The enzyme was stable for at least 8 weeks when stored at
-80[deg] C. The occurrence of cis-trans-isomerization suggests that
cis-zeatin and cis-zeatin riboside formed by tRNA degradation could be
precursors of biologically active cytokinins.
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