A Beta-Turn Rich Barley Seed Protein Is Correctly Folded in Escherichia-coli
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Tartalom: http://real.mtak.hu/5230/
Archívum: REAL
Gyűjtemény: Status = Published
Subject = Q Science / természettudomány: QH Natural history / természetrajz: QH301 Biology / biológia: QH3011 Biochemistry / biokémia
Subject = Q Science / természettudomány: QR Microbiology / mikrobiológia
Subject = Q Science / természettudomány: QH Natural history / természetrajz: QH301 Biology / biológia: QH3015 Molecular biology / molekuláris biológia
Type = Article
Cím:
A Beta-Turn Rich Barley Seed Protein Is Correctly Folded in Escherichia-coli
Létrehozó:
Tamás, László
Greenfield, J.
Halford, N. G.
Dátum:
1994
Téma:
QH3011 Biochemistry / biokémia
QH3015 Molecular biology / molekuláris biológia
QR Microbiology / mikrobiológia
Tartalmi leírás:
Wild-type and cysteine-containing mutant C hordeins from barley were expressed in Escherichia coli at high levels (greater-than-or-equal-to 30 mg/liter). N-terminal sequence analysis, SDS-PAGE, RP-HPLC, cd spectroscopy, and small angle X-ray scattering demonstrated that their physicochemical properties were similar to those of C hordeins isolated from barley grain. This indicates that the expressed proteins were correctly folded. The cysteine-containing mutant showed evidence of polymer formation in E. coli, nonreduced preparations of the protein showing the presence of polymers that were replaced by a single protein when a reducing agent was added. (C) 1994 Academic Press, Inc.
Típus:
Article
PeerReviewed
Formátum:
text
Azonosító:
Tamás, László and Greenfield, J. and Halford, N. G. (1994) A Beta-Turn Rich Barley Seed Protein Is Correctly Folded in Escherichia-coli. PROTEIN EXPRESSION AND PURIFICATION, 5 (4). pp. 357-363. ISSN 1046-5928
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