A β-Turn Rich Barley Seed Protein Is Correctly Folded in Escherichia coli

L. Tamas; J. Greenfield; N. G. Halford; A. S. Tatham; P. R. Shewry

doi:10.1006/prep.1994.1052

A β-Turn Rich Barley Seed Protein Is Correctly Folded in Escherichia coli

L. Tamas^*, J. Greenfield, N. G. Halford, A. S. Tatham, P. R. Shewry

^*Awdur cyfatebol y gwaith hwn

Allbwn ymchwil: Cyfraniad at gyfnodolyn › Erthygl › adolygiad gan gymheiriaid

21 Dyfyniadau (Scopus)

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Wild-type and cysteine-containing mutant C hordeins from barley were expressed in Escherichia coli at high levels (≥ 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.

Iaith wreiddiol	Saesneg
Tudalennau (o-i)	357-363
Nifer y tudalennau	7
Cyfnodolyn	Protein Expression and Purification
Cyfrol	5
Rhif cyhoeddi	4
Dynodwyr Gwrthrych Digidol (DOIs)	https://doi.org/10.1006/prep.1994.1052
Statws	Cyhoeddwyd - Awst 1994
Cyhoeddwyd yn allanol	Ie

Mynediad at Ddogfen

10.1006/prep.1994.1052

Ffeiliau eraill a chysylltiadau

Dolen i’r cyhoeddiad yn Scopus

Dyfynnu hyn

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title = "A β-Turn Rich Barley Seed Protein Is Correctly Folded in Escherichia coli",

abstract = "Wild-type and cysteine-containing mutant C hordeins from barley were expressed in Escherichia coli at high levels (≥ 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.",

author = "L. Tamas and J. Greenfield and Halford, \{N. G.\} and Tatham, \{A. S.\} and Shewry, \{P. R.\}",

year = "1994",

month = aug,

doi = "10.1006/prep.1994.1052",

language = "English",

volume = "5",

pages = "357--363",

journal = "Protein Expression and Purification",

issn = "1046-5928",

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T1 - A β-Turn Rich Barley Seed Protein Is Correctly Folded in Escherichia coli

AU - Tamas, L.

AU - Greenfield, J.

AU - Halford, N. G.

AU - Tatham, A. S.

AU - Shewry, P. R.

PY - 1994/8

Y1 - 1994/8

N2 - Wild-type and cysteine-containing mutant C hordeins from barley were expressed in Escherichia coli at high levels (≥ 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.

AB - Wild-type and cysteine-containing mutant C hordeins from barley were expressed in Escherichia coli at high levels (≥ 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.

UR - https://www.scopus.com/pages/publications/0028484070

U2 - 10.1006/prep.1994.1052

DO - 10.1006/prep.1994.1052

M3 - Article

C2 - 7950382

AN - SCOPUS:0028484070

SN - 1046-5928

VL - 5

SP - 357

EP - 363

JO - Protein Expression and Purification

JF - Protein Expression and Purification

IS - 4

ER -