PMID: 1201000Sep 1, 1975Paper

Structural studies on wheat (Triticum aestivum) proteins lacking phenylalanine and histidine residues

The Biochemical Journal
D G Redman

Abstract

1. Three very similar proteins, each of approx. 120 amino acid residues but lacking phenylalanine and histidine, were isolated from wheat (Triticum aestivum) flour in sufficient quantities for further structural studies. 2. Each protein, after reduction and carboxymethylation, was cleaved at the three methionine residues with CNBr to give four major peptides, which were isolated. These peptides are suitable for future sequencing studies, as the sums of their amino acid compositions are in good agreement with those of the whole proteins. 3. The N- and C-terminal peptides were identified. 4. Evidence from amino acid analyses, N-terminal amino acids and electrophoretic mobilities of the peptides suggests a high degree of homology between the proteins. Definite differences in C-terminal amino acids and the number of glycine, alanine and arginine residues were found in the C-terminal peptides.

Citations

Jan 15, 1980·Analytical Biochemistry·M A KirkmanW R Mills
Nov 1, 1976·TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik·L Vittozzi, V Silano
Dec 29, 1977·Molecular and Cellular Biochemistry·V SilanoV Buonocore

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