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Expression of Pisum sativum SAD polypeptides in production hosts and in planta: Tetrameric organization of the protein
Örebro universitet, Akademin för naturvetenskap och teknik.ORCID-id: 0000-0001-9713-2365
Örebro universitet, Akademin för naturvetenskap och teknik.
Örebro universitet, Hälsoakademin.
Vise andre og tillknytning
2009 (engelsk)Inngår i: Protein Expression and Purification, ISSN 1046-5928, E-ISSN 1096-0279, Vol. 63, nr 1, s. 18-25Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

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.

sted, utgiver, år, opplag, sider
Amsterdam, 2009. Vol. 63, nr 1, s. 18-25
HSV kategori
Forskningsprogram
Biokemi
Identifikatorer
URN: urn:nbn:se:oru:diva-4628DOI: 10.1016/j.pep.2008.09.004ISI: 000261035100004PubMedID: 18814850OAI: oai:DiVA.org:oru-4628DiVA, id: diva2:138927
Tilgjengelig fra: 2008-10-14 Laget: 2008-10-14 Sist oppdatert: 2018-01-13bibliografisk kontrollert

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Scherbak, NikolaiAla-Häivälä, AnneliStrid, HiljaStrid, Åke

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