Linked Life Data

15134653

Source:http://linkedlifedata.com/resource/pubmed/id/15134653

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2004-5-11
pubmed:databankReference
pubmed:abstractText
Soybean 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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
6
pubmed:volume
1698
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
203-12
pubmed:dateRevised
2009-6-25
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
The expression and processing of two recombinant 2S albumins from soybean (Glycine max) in the yeast Pichia pastoris.
pubmed:affiliation
School of Biology, University of Nottingham, University Park, Nottingham NG7 2RD, UK.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't