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Expression of Pisum sativum SAD polypeptides in production hosts and in planta: Tetrameric organization of the protein
Örebro University, School of Science and Technology.ORCID iD: 0000-0001-9713-2365
Örebro University, School of Science and Technology.
Örebro University, School of Health and Medical Sciences.
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2009 (English)In: Protein Expression and Purification, ISSN 1046-5928, E-ISSN 1096-0279, Vol. 63, no 1, p. 18-25Article in journal (Refereed) 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.

Place, publisher, year, edition, pages
Amsterdam, 2009. Vol. 63, no 1, p. 18-25
National Category
Biochemistry and Molecular Biology Other Basic Medicine Medical and Health Sciences
Research subject
Biochemistry
Identifiers
URN: urn:nbn:se:oru:diva-4628DOI: 10.1016/j.pep.2008.09.004ISI: 000261035100004PubMedID: 18814850OAI: oai:DiVA.org:oru-4628DiVA, id: diva2:138927
Available from: 2008-10-14 Created: 2008-10-14 Last updated: 2018-01-13Bibliographically approved

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Scherbak, NikolaiAla-Häivälä, AnneliStrid, HiljaStrid, Åke

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Protein Expression and Purification
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