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pubmed-article:15134653pubmed:abstractTextSoybean seeds contain two 2S albumin storage proteins (AL1 and AL3) which may contribute to their industrial processing quality and allergenicity. We show that these proteins (AL1 and AL3) are well expressed by the methylotrophic yeast Pichia pastoris and that one of the secreted proteins (AL3) has a similar conformation and stability to that purified from soybean seeds. Further, we show that the subunits are post-translationally processed within the same loop region as the native protein but with some differences in the precise sites. This internal processing provides useful information on the endoproteolytic activity in P. pastoris. We also show that, similar to many plant allergens, the 2S albumins from soybean are stable to heat and chemical treatments.lld:pubmed
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pubmed-article:15134653pubmed:dateRevised2009-6-25lld:pubmed
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pubmed-article:15134653pubmed:articleTitleThe expression and processing of two recombinant 2S albumins from soybean (Glycine max) in the yeast Pichia pastoris.lld:pubmed
pubmed-article:15134653pubmed:affiliationSchool of Biology, University of Nottingham, University Park, Nottingham NG7 2RD, UK.lld:pubmed
pubmed-article:15134653pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:15134653pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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