N-terminal amino acid sequence homology of storage protein components from barley and a diploid wheat

Shewry, Peter R.; Autran, J.C.; Nimmo, C. C.; Lew, Ellen J-L.; Kasarda, Donald D.

doi:10.1038/286520a0

Cited by 82 publications

(20 citation statements)

References 19 publications

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“…This group of polypeptides is characterized by its solubility in aqueous alcohol and can be separated into several components using electrophoretic techniques (for recent reviews see 6, 13, (20). This has been corroborated by the demonstration, that y3-gliadin from wheat T. monococcum) and C hordein from barley are homologous (22).…”

Section: Introductionmentioning

confidence: 72%

Partial amino acid sequence from hordein polypeptide B1

Schmitt

Svendsen

1980

Carlsberg Res. Commun.

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Hordein polypeptide B1 has been cleaved with CNBr, Staphylococcus V8 protease and trypsin under denaturing conditions. Fragments have been isolated and examined by amino acid analysis and sequence determination. Amino acid residues were distributed irregularly along the B I polypeptide chain with no indication of large Glx/Pro clusters. The single sequences presented account for about one fourth of the molecule. Two homologous but different tryptic peptides indicate either the presence of different B 1 molecules or internal sequence repetition.

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Section: Introductionmentioning

confidence: 72%

Partial amino acid sequence from hordein polypeptide B1

Schmitt

Svendsen

1980

Carlsberg Res. Commun.

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“…If it is assumed that the rate of evolution of the NH2-terminal regions of the enzyme is equivalent to that of the fibrinopeptides, which at 9 amino acid substitutions per amino acid site per 109 year are the fastest evolving peptides so far characterized [ 10], it may be calculated [ 11 ] that gene duplication occurred at least 8 X 106 years ago.…”

Section: Resultsmentioning

confidence: 99%

Amino acid sequence homology in two 1,3;1,4‐β‐glucan endohydrolases from germinating barley (hordeum vulgare)

Woodward

Morgan

1982

FEBS Letters

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“…4a, part a) have major components with Mr values of about 52000-54000 (as determined by sedimentation equilibrium ultracentrifugation [60] and intrinsic viscosity measurements in 5.9 M-guanidinium chloride [61]). Partial amino acid sequences determined directly [62][63][64] and deduced from cloned cDNAs [65,66] show unique N-terminal and C-terminal domains of 12 andK 6 residues respectively, flanking a repetitive domain calculated (from the Mr values) as consisting of over 400 residues (Fig. 4b).…”

Section: Hmw Prolamins Of Barley and Ryementioning

confidence: 99%