Electrophoretic characterisation of fractions collected from gluten protein extracts subjected to size-exclusion high-performance liquid chromatography

被引:55
作者
Larroque, OR
Gianibelli, MC
Batey, IL
MacRitchie, F
机构
[1] CSIRO,DIV PLANT IND,N RYDE,NSW 2113,AUSTRALIA
[2] UNIV WESTERN SYDNEY,RICHMOND,NSW,AUSTRALIA
[3] NATL UNIV LA PLATA,RA-1900 LA PLATA,ARGENTINA
[4] WHEAT QUAL CRC,N RYDE,NSW,AUSTRALIA
关键词
wheat endosperm proteins; polymeric protein; monomeric protein; high performance liquid chromatography; sodium dodecyl sulfate-polyacrylamide gel electrophoresis; gel scanning;
D O I
10.1002/elps.1150180706
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
The electrophoretic analysis by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE; reduced and unreduced) of fractions, collected from a size exclusion-high performance liquid chromatography (SE-HPLC) separation of gluten proteins using a column with pare size of around 400 Angstrom, showed clear resolution for the seven elution ranges studied in two Australian bread wheat lines. Polymeric proteins - high molecular weight (HMW) glutenin subunits, low molecular weight (LMW) glutenin subunits, HMW albumins and some modified omega-gliadins - appeared exclusively in the region within the first peak of the chromatogram (fractions 1 to 5), the limit being a region that resolved as a small peak before the large peal; of gliadins and where some omega-gliadins eluted. A larger proportion of HMW glutenin subunits and B subunits contributed to polymer formation of higher molecular weight. The polymer size decreased as the proportion of the other protein components increased.
引用
收藏
页码:1064 / 1067
页数:4
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