Cereal Chem 72:356-359  |  VIEW ARTICLE

C-Terminal and Internal Sequences of a Low Molecular Weight (LMW-s) Type of Glutenin Subunit.

W. H. Vensel, G. E. Tarr, and D. D. Kasarda. Copyright 1995 by the American Association of Cereal Chemists, Inc. 

Amino acid sequences have been determined for a 25-residue C- terminal peptide and for two 9-residue peptides, all derived from cyanogen bromide fragmentation of a low molecular weight glutenin subunit (LMW-GS) with the N-terminal sequence: serine- histidine-isoleucine-proline-glycine- (LMW-s type). Previously, only N-terminal amino acid sequences have been available for LMW-s types, which appear to be the predominant LMW-GS type in hexaploid and tetraploid wheats. N-terminal sequences and complete sequences based on DNA sequences have been available, however, for subunits of the LMW-m type. These have the N- terminal sequence: methionine-glutamic acid-threonine-serine- cysteine-. All three peptides prepared from the LMW-s type subunit showed strong sequence similarities to LMW-m type subunits from hexaploid and tetraploid bread wheats. The 25-residue C-terminal fragment was 80% identical to DNA- derived sequences of specific LMW-m types. Two of the peptides contained cysteine and showed homology around these cysteines with LMW-m type sequences. The results support the basic similarity between LMW-s and LMW- m glutenin subunits.