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• W1978779709 abstract "Endosperm-specific low-molecular-weight (LMW) glutenins are an important component of the polymeric gluten and, as such, play a key role in end-use functionality. Reports of N-terminal amino acid sequences of LMW glutenin fractions revealed that they have either a methionine or a serine residue at the first position of the mature peptide. These subunits were therefore called LMW-m and LMW-s type glutenins. A gene that is predicted to encode a LMW glutenin subunit having an isoleucine amino acid residue at position one of the mature protein was amplified and cloned from extra strong bread wheat cultivar Glenlea (pGH3.1). The predicted N-terminal sequence of this gene is truncated as compared to the m-type and s-type. The gene still codes for the expected number of eight cysteine residues which are all located in the C-terminal region. We propose to call it LMW-i based on the same nomenclature. Analysis of 277 doubled haploid lines derived from a single cross showed perfect co-segregation of the cloned PCR fragment with a rare LMW glutenin called LMW-50. The gene was subcloned in an expression vector and the protein was expressed in E. coli. Western blot analysis using a prolamin-specific monoclonal antibody confirmed the co-migration of the cloned protein with LMW-50 from Glenlea." @default.
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• W1978779709 date "2001-03-01" @default.
• W1978779709 modified "2023-10-15" @default.
• W1978779709 title "Cloning and Expression of a LMW-i Glutenin Gene" @default.
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• W1978779709 doi "https://doi.org/10.1006/jcrs.2000.0359" @default.
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