Purification and partial characterization of a gibberellin 2β-hydroxylase fromPhaseolus vulgaris
✍ Scribed by Valerie A. Smith; Jake MacMillan
- Publisher
- Springer
- Year
- 1983
- Tongue
- English
- Weight
- 630 KB
- Volume
- 2
- Category
- Article
- ISSN
- 0721-7595
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The gibberellin (GA) 2fl-hydroxylases in mature and immature seeds of Pisum sativum have been partially purified and characterised. The enzymes are unstable when stored below pH 7.0 or in the absence of a thiol reagent. The optimum assay pH is between 7.4 and 7.8 and activity is dependent upon the p
An intracellular enzyme, D(-)-fl-hydroxybutyric acid dehydrogenase involved in an intracellular poly-D(-)-fl-hydroxybutyric acid degradation was isolated from a facultative methylotrophic bacterium, P s e u d o m o n a s 135, grown on methanol as a sole carbon and energy source. This enzyme was part