Characterisation of a novel high Mr glutenin subunit encoded by chromosome 1D of bread wheat

F. Buonocore; D. R. Hickman; C. Caporale; E. Porceddu; D. Lafiandra; A. S. Tatham; P. R. Shewry

doi:10.1006/jcrs.1996.0005

Characterisation of a novel high M_r glutenin subunit encoded by chromosome 1D of bread wheat

F. Buonocore^*, D. R. Hickman, C. Caporale, E. Porceddu, D. Lafiandra, A. S. Tatham, P. R. Shewry

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

9 Citations (Scopus)

Abstract

A high M_r subunit of wheat glutenin (1Dx2·2*), having an unusually high M_r (approximately 110000), was purified using a combination of preparative isoelectric focusing and reversed-phase high performance liquid chromatography. Comparison of its N-terminal sequence and amino acid composition with those of the allelic subunit 1Dx2 indicate that its greater M_r could be due to the presence of a larger central repetitive domain. Spectrofluorimetric and circular dichroism analyses suggest that an increase in the length of this domain does not affect the conformational properties of the subunit.

Original language	English
Pages (from-to)	55-60
Number of pages	6
Journal	Journal of Cereal Science
Volume	23
Issue number	1
DOIs	https://doi.org/10.1006/jcrs.1996.0005
Publication status	Published - Jan 1996
Externally published	Yes

Keywords

High M glutenin subunits

Access to Document

10.1006/jcrs.1996.0005

Cite this

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title = "Characterisation of a novel high Mr glutenin subunit encoded by chromosome 1D of bread wheat",

abstract = "A high Mr subunit of wheat glutenin (1Dx2·2*), having an unusually high Mr (approximately 110000), was purified using a combination of preparative isoelectric focusing and reversed-phase high performance liquid chromatography. Comparison of its N-terminal sequence and amino acid composition with those of the allelic subunit 1Dx2 indicate that its greater Mr could be due to the presence of a larger central repetitive domain. Spectrofluorimetric and circular dichroism analyses suggest that an increase in the length of this domain does not affect the conformational properties of the subunit.",

keywords = "High M glutenin subunits",

author = "F. Buonocore and Hickman, {D. R.} and C. Caporale and E. Porceddu and D. Lafiandra and Tatham, {A. S.} and Shewry, {P. R.}",

year = "1996",

month = jan,

doi = "10.1006/jcrs.1996.0005",

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AU - Buonocore, F.

AU - Hickman, D. R.

AU - Caporale, C.

AU - Porceddu, E.

AU - Lafiandra, D.

AU - Tatham, A. S.

AU - Shewry, P. R.

PY - 1996/1

Y1 - 1996/1

N2 - A high Mr subunit of wheat glutenin (1Dx2·2*), having an unusually high Mr (approximately 110000), was purified using a combination of preparative isoelectric focusing and reversed-phase high performance liquid chromatography. Comparison of its N-terminal sequence and amino acid composition with those of the allelic subunit 1Dx2 indicate that its greater Mr could be due to the presence of a larger central repetitive domain. Spectrofluorimetric and circular dichroism analyses suggest that an increase in the length of this domain does not affect the conformational properties of the subunit.

AB - A high Mr subunit of wheat glutenin (1Dx2·2*), having an unusually high Mr (approximately 110000), was purified using a combination of preparative isoelectric focusing and reversed-phase high performance liquid chromatography. Comparison of its N-terminal sequence and amino acid composition with those of the allelic subunit 1Dx2 indicate that its greater Mr could be due to the presence of a larger central repetitive domain. Spectrofluorimetric and circular dichroism analyses suggest that an increase in the length of this domain does not affect the conformational properties of the subunit.

KW - High M glutenin subunits

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U2 - 10.1006/jcrs.1996.0005

DO - 10.1006/jcrs.1996.0005

M3 - Article

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SN - 0733-5210

VL - 23

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EP - 60

JO - Journal of Cereal Science

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