| Tartalom: |
http://real.mtak.hu/5230/ |
| Archívum: |
MTA Könyvtár |
| Gyűjtemény: |
Status = Published
Type = Article
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| Cím: |
A Beta-Turn Rich Barley Seed Protein Is Correctly Folded in Escherichia-coli
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| Létrehozó: |
Tamás, László
Greenfield, J.
Halford, N. G.
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| Kiadó: |
Elsevier
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| Dátum: |
1994
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| Téma: |
QH3011 Biochemistry / biokémia
QH3015 Molecular biology / molekuláris biológia
QR Microbiology / mikrobiológia
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| 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.
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| Típus: |
Article
PeerReviewed
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| Formátum: |
text
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| 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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