Abstract:
:In Pisum sativum, the short-chain alcohol dehydrogenase-like protein (SAD) gene family consists of at least three members (SAD-A, -B, and -C). Expression of two of these genes (SAD-A and -C) in Escherichia coli or Pichia pastoris resulted in full-length soluble proteins. Purified SAD-A was used as antigen for antibody production in rabbits. With these antibodies the recombinant SAD-C protein (which was most highly expressed of the two isoforms) was shown to be a tetramer consisting of a dimer of dimers. The SAD genes are transiently expressed in plants by short exposures to ultraviolet-B radiation (UV-B), as judged by northern blotting. In turn, mRNA accumulation leads to formation of SAD protein in leaf and stem tissue upon prolonged UV-B irradiation.
journal_name
Protein Expr Purifjournal_title
Protein expression and purificationauthors
Scherbak N,Brosché M,Ala-Häivälä A,Strid H,Ohrfelt A,Nilsson F,Strid Adoi
10.1016/j.pep.2008.09.004subject
Has Abstractpub_date
2009-01-01 00:00:00pages
18-25issue
1eissn
1046-5928issn
1096-0279pii
S1046-5928(08)00230-1journal_volume
63pub_type
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