| Literature DB >> 15849430 |
Masahiro Tamoi1, Miki Nagaoka, Shigeru Shigeoka.
Abstract
Here we report on the production of functional recombinant SBPase of Chlamydomonas sp. W80 in Escherichia coli and the one-step purification of a polyhistidine-tagged fusion protein. The polyclonal antibody was raised against purified recombinant enzyme and cross-reacted with crude SBPase from Chlamydomonas, spinach, tobacco, and Arabidopsis leaves. Further, we investigated the levels of protein and activity of SBPase in different tissues of Arabidopsis plants.Entities:
Mesh:
Substances:
Year: 2005 PMID: 15849430 DOI: 10.1271/bbb.69.848
Source DB: PubMed Journal: Biosci Biotechnol Biochem ISSN: 0916-8451 Impact factor: 2.043