Antisense-mediated suppression of C-hordein biosynthesis in the barley grain results in correlated changes in the transcriptome, protein profile, and amino acid composition

SUMMARYThe amino acid composition of barley grain was studied during the maturation of the grain and during germination of the mature grain. Samples of the variety Proctor, grown at two nitrogen levels in each of the years 1969 and 1970, were analysed together with one sample of Sultan grown in 1970. It was found that during maturation the proportions of glutamic acid and proline increased and that the levels of these amino acids were highest in those samples with the highest total protein content. During ripening the proportions of lysine, alanine, aspartic acid, threonine and glycine decreased. On germination the proportions of glutamic acid and proline rapidly decreased whilst aspartic acid, lysine, alanine and glycine increased.The nutritive value of ripe barley grain is limited by its low lysine content. Whilst the germination process increases the level of lysine it is suggested that this does not increase the nutritional value of the grain due to the low level of cystine in the germinated grain.

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Varietal differences in the amino acid composition of barley grain during development and under varying nitrogen supply

Journal of the Science of Food and Agriculture ◽

10.1002/jsfa.2740250812 ◽

1974 ◽

Vol 25 (8) ◽

pp. 963-972 ◽

Cited By ~ 16

Author(s):

Anthony P. Rhodes ◽

John C. Mathers

Keyword(s):

Amino Acid ◽

Amino Acid Composition ◽

Acid Composition ◽

Barley Grain ◽

Nitrogen Supply ◽

Varietal Differences

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Targeted modification of storage protein content resulting in improved amino acid composition of barley grain

Transgenic Research ◽

10.1007/s11248-015-9911-7 ◽

2015 ◽

Vol 25 (1) ◽

pp. 19-31 ◽

Cited By ~ 8

Author(s):

Md. S. I. Sikdar ◽

S. Bowra ◽

D. Schmidt ◽

G. Dionisio ◽

P. B. Holm ◽

...

Keyword(s):

Amino Acid ◽

Amino Acid Composition ◽

Protein Content ◽

Acid Composition ◽

Storage Protein ◽

Barley Grain

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Studies on the structure of sphingomyelinase. Amino acid composition and heterogeneity on isoelectric focusing

Biochemical Journal ◽

10.1042/bj2090291 ◽

1983 ◽

Vol 209 (2) ◽

pp. 291-297 ◽

Cited By ~ 15

Author(s):

C S Jones ◽

P Shankaran ◽

D J Davidson ◽

A Poulos ◽

J W Callahan

Keyword(s):

Amino Acid ◽

Amino Acid Composition ◽

Acid Composition ◽

Isoelectric Focusing ◽

Protein Profile ◽

Minor Component ◽

Intact Protein ◽

Amino Acid Residues ◽

Apparent Homogeneity ◽

A Minor

Sphingomyelinase, purified to apparent homogeneity from human placenta, is an acidic protein, as judged from its amino acid composition and by isoelectric focusing of the carboxymethylated protein. The amino acid composition is characterized by an approximately equal content of hydrophobic and polar amino acid residues. The reduced-alkylated polypeptides were separated into two groups. Most of the polypeptides were heterogeneous with pI values of 4.4-5.0, but an additional more minor component was observed at pI 5.4. Liquid isoelectric focusing resolved the purified enzyme into a single major component (pI 4.7-4.8), a minor component (pI 5.0-5.4) and a plateau region of activity (pI 6-7). On thin-layer isoelectric focusing, the protein profile obtained from each of these regions was the same. In addition, the substrate specificity, Km values and effect of inhibitory substances were identical. We conclude that sphingomyelinase is an acidic, microheterogeneous protein that likely exists as a holopolymer of a single major polypeptide chain. the heterogeneity of the intact protein on isoelectric focusing appears to reflect this microheterogeneity, which is influenced by a tendency to associate with itself and with detergents such as Triton X-100.

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