Two-Dimensional Gel Mapping and N-Terminal Sequencing of LMW-Glutenin Subunits

Low-molecular-weight glutenin subunits from the wheat (Triticum aestivum L.) cultivar ‘Chinese Spring’ were mapped using two dimensional electrophoresis (isoelectric focusing versus SDS-polyacrylamide gel electrophoresis). Protein spots were electroblotted on to polyvinylidene difluoride membrane an...

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Bibliographic Details
Published in:Journal of experimental botany 1989-09, Vol.40 (9), p.1015-1020
Main Authors: TAO, H. PEGGY, KASARDA, DONALD D.
Format: Article
Language:English
Subjects:
Agriculture
Albumins
amino acid sequences
Amino acids
electroblotting
Electrophoresis
Gels
Genes
Glutenin
Polymers
Proteins
Sequencing
Wheat
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Summary:Low-molecular-weight glutenin subunits from the wheat (Triticum aestivum L.) cultivar ‘Chinese Spring’ were mapped using two dimensional electrophoresis (isoelectric focusing versus SDS-polyacrylamide gel electrophoresis). Protein spots were electroblotted on to polyvinylidene difluoride membrane and characterized by N-terminal amino acid sequencing. Most of the proteins that had accessible N-termini gave sequences in agreement with known sequences for low-molecular-weight glutenins, α-type gliadins, and γ-type gliadins. Two variants which have not been seen in direct sequencing before were found. The glutenin starting material was also reduced, alkylated, and partially fractionated by reverse-phase high performance liquid chromatography. Sequencing of these fractions, each of which contained a mixture of proteins, confirmed the presence of the glutenin variants found in the spot sequencing.
ISSN:0022-0957
1460-2431
DOI:10.1093/jxb/40.9.1015