| Literature DB >> 16668210 |
J M Bruneau1, A C Worrell, B Cambou, D Lando, T A Voelker.
Abstract
We have purified the protein for the enzyme sucrose phosphate synthase (SPS) from corn (Zea mays) leaves. Partially purified SPS protein was used to generate specific monoclonal antibodies. The following immunoaffinity chromatography allowed the isolation of pure SPS protein. The apparent molecular mass of the SPS polypeptide is 138 kilodaltons. By immunoblot, an SPS antigen was found to accumulate in mature leaves. SPS protein levels remain constant during the day/night cycle. The observed diurnal fluctuation of extractable enzyme activity, therefore, must be caused by modification of the specific activity of SPS in vivo.Entities:
Year: 1991 PMID: 16668210 PMCID: PMC1080794 DOI: 10.1104/pp.96.2.473
Source DB: PubMed Journal: Plant Physiol ISSN: 0032-0889 Impact factor: 8.340