Disulphide bonds of adjacent cysteine residues in low molecular weight subunits of wheat glutenin

被引:133
|
作者
Muller, S
Vensel, WH
Kasarda, DD
Kohler, P
Wieser, H
机构
[1] Deutsch Forsch Anstalt Lebensmittelchem, D-85748 Garching, Germany
[2] Kurt Hess Inst Mehl & Eiweissforsch, D-85748 Garching, Germany
[3] Western Reg Res Ctr, Albany, CA 94710 USA
关键词
wheat gluten; LMW subunits; disulphide bonds; adjacent cysteines;
D O I
10.1006/jcrs.1997.0158
中图分类号
TS2 [食品工业];
学科分类号
0832 ;
摘要
The adjacent cysteine residues C-f1 and C-f2 located in the homologous sequence division III of LMW subunits of glutenin, and of alpha- and gamma-gliadins are important elements of the disulphide structure of these proteins. Two different analytical approaches were used to assign the disulphide linkages of the -Cys-Cys- sequence found in four cystine-containing peptides derived from LMW subunits of glutenin. Direct Edman degradation of the acetylated and cyanogen bromide treated peptide with detection of di-PTH-cystine was one method. Partial reduction of peptides with Tris(2-carboxyethyl)phosphine hydrochloride, subsequent separation of fragments by RP-HPLC, alkylation with iodoacetamide and sequence analysis was the second method. Both these methodologies gave identical results. It was shown that the first of the adjacent cysteines (C-f1) is linked with another cysteine residue of division III (C-c) and that the second one of the pair (C-f2) is linked with a cysteine residue in the C-terminal division V (C-y) of the primary structure. A model for the complete disulphide structure of LMW subunits is presented. (C) 1998 Academic Press Limited.
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页码:109 / 116
页数:8
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