| Literature DB >> 16666288 |
J M Chatfield1, D J Armstrong.
Abstract
Cytokinin oxidase activity from Phaseolus vulgaris cv Great Northern callus cultures exhibited affinity for the lectin concanavalin A. Over 80% of the activity extracted from the callus tissue bound to a concanavalin A-Sepharose 4B column. The bound activity was eluted from the column by the addition of methylmannose to the eluting buffer. On the basis of this result, it appears that most of the cyokinin oxidase activity present in Great Northern callus cultures exists in the form of a glycoprotein. The apparent pI of this enzyme, as estimated by chromatofocusing, is approximately 5.0.Entities:
Year: 1988 PMID: 16666288 PMCID: PMC1055561 DOI: 10.1104/pp.88.2.245
Source DB: PubMed Journal: Plant Physiol ISSN: 0032-0889 Impact factor: 8.340