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.
journal_name
Plant Physioljournal_title
Plant physiologyauthors
Bruneau JM,Worrell AC,Cambou B,Lando D,Voelker TAdoi
10.1104/pp.96.2.473subject
Has Abstractpub_date
1991-06-01 00:00:00pages
473-8issue
2eissn
0032-0889issn
1532-2548journal_volume
96pub_type
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