Environmentally Induced Changes in Amino Acid Composition in the Grain of Durum Wheat Grown under Different Water and Temperature Regimes in a Mediterranean Environment

2007 ◽  
Vol 55 (20) ◽  
pp. 8144-8151 ◽  
Author(s):  
Luis F. García del Moral ◽  
Yahia Rharrabti ◽  
Vanessa Martos ◽  
Conxita Royo
1970 ◽  
Vol 50 (1) ◽  
pp. 9-14 ◽  
Author(s):  
C. H. CHEN ◽  
W. BUSHUK

Solubility characteristics and amino acid composition of the endosperm proteins of one line of Triticale, its durum wheat and rye parent cultivars, and one cultivar of hard red spring wheat were compared. Quantitative distribution of the soluble protein fractions and amino acid compositions showed that the proteins of Triticale are intermediate in these properties between analogous properties of the proteins of its durum wheat and rye parents. The major differences between the hard red spring wheat and the other three species were its lower content of water-soluble proteins and higher content of insoluble or gluten proteins. This appears lo be the main reason for the superior breadmaking quality of the hard red spring wheat cultivar compared with the other species used in this study.


1975 ◽  
Vol 55 (2) ◽  
pp. 537-546 ◽  
Author(s):  
J. E. DEXTER ◽  
B. L. DRONZEK

The amino acid composition of the maturing endosperm of a triticale (X Triticosecale Wittmack) designated line 6A190 and its rye (Secale cereale L.) and durum wheat (Triticum durum Desf.) parents were determined. In all three cereals, rapid changes occurred during development in the free amino acid levels and in the nature of the endosperm proteins. The composition of the free amino acids of triticale more closely resembled the rye parent than the durum wheat parent throughout endosperm development. The amino acid composition of the proteins and peptides of triticale was intermediate to the rye and durum wheat parents at all stages of development.


1987 ◽  
Vol 242 (1) ◽  
pp. 245-251 ◽  
Author(s):  
N C Khanna ◽  
M Tokuda ◽  
D M Waisman

Calregulins were purified from bovine, rabbit and chicken liver, and their structural properties were compared. Significant differences between the three calregulins include a lower Mr for chicken calregulin (57,000) than for rabbit and bovine calregulin (63,000), and the glycosylation of only bovine calregulin. Amino acid composition and peptide maps of the three calregulins were very similar. No major differences were detected in the Ca2+-binding properties of the three proteins. Zn2+-induced changes in calregulin conformation and hydrophobicity monitored by intrinsic protein fluorescence and the hydrophobic fluorescent probe 8-anilino-1-naphthalenesulphonate were very similar, suggesting that the Zn2+-dependent increase in the hydrophobicity of bovine, rabbit and chicken calregulin was conserved. These studies more fully define what is a calregulin, demonstrate that calregulin is a relatively invariant constituent of vertebrate liver, and indicate that calregulin structure has been highly conserved in bovine, chicken and rabbit liver.


2015 ◽  
Vol 40 (3) ◽  
pp. 247-257 ◽  
Author(s):  
GERALDINE D. RYAN ◽  
EMMA V. A. SYLVESTER ◽  
BARRY J. SHELP ◽  
JONATHAN A. NEWMAN

2014 ◽  
Author(s):  
Alexandra Jayne Kermack ◽  
Ying Cheong ◽  
Nick Brook ◽  
Nick Macklon ◽  
Franchesca D Houghton

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