The Extraction, Solubility, and Characterization of Two Groups of Barley Storage Polypeptides

Shewry, Peter R.; J, Field; Kirkman, M. A.; Faulks, Audrey J.; Miflin, B. J.

doi:10.1093/jxb/31.2.393

Cited by 112 publications

(57 citation statements)

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“…Amino acid compositions (residues/mol) of individual HMW, S-poor and S-rich prolamins Based on sequences in [43,88,93,111,112]. The data for C hordein are calculated on the basis of the Mr (52570) determined by sedimention equilibrium ultracentrifugation, as described in [60]. Absolute Mr values are given for the other proteins.…”

Section: The Prolamins Of Wheat Barley and Ryementioning

confidence: 99%

“…Their Mr values by SDS/PAGE vary from about 55000 to 70000, but the fractions which have been studied in detail (Fig. 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.…”

Section: Hmw Prolamins Of Barley and Ryementioning

confidence: 99%

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The prolamin storage proteins of cereal seeds: structure and evolution

Shewry

Tatham

1990

Biochemical Journal

636

421

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Section: The Prolamins Of Wheat Barley and Ryementioning

confidence: 99%

Section: Hmw Prolamins Of Barley and Ryementioning

confidence: 99%

The prolamin storage proteins of cereal seeds: structure and evolution

Shewry

Tatham

1990

Biochemical Journal

636

421

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“…Mean prolamin content of 50.6% in the present genotypes was greater compared to 46.6% reported by Giuberti et al (2012), and compared to mean albumin and globulin contents in the present study (17.9% and 9.0%, respectively). Gabert et al (1996) reported greater proportions of Lys and lower proportions of Glu in barley protein, when Lys-poor prolamin fraction decreased and Lys-rich glutelin fraction increased (Shewry et al, 1980;Gabert et al, 1996). Thus, lower mean Lys and greater mean Leu, Phe and Pro contents in the assay genotypes compared to values reported by NRC (2012) are reflected in a greater proportion of prolamin and lower proportions of albumin and globulin.…”

Section: Discussionmentioning

confidence: 99%

Standardized ileal digestibility of amino acids in eight genotypes of barley fed to growing pigs

Spindler

Mosenthin

Rosenfelder

et al. 2016

animal

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To determine chemical composition, physical characteristics and standardized ileal digestibility (SID) of CP and amino acids (AA) in eight current hulled barley genotypes, an experiment with growing pigs has been conducted. These genotypes included Yool, Campanile, Lomerit, Travira, Anisette, Canberra, Metaxa and Fridericus. Growing barrows with an average initial BW of 30 ± 2 kg were surgically fitted with simple T-cannulas at the distal ileum, and allotted to an 8 × 9 Youden square design with eight periods of 6 days each and nine pigs. Barley was the sole dietary source of CP and AA. On average, the eight genotypes contained on as-fed basis 10.7% CP, 15.2% total non-starch polysaccharides (NSP), 17.1% NDF and 4.1% β-glucan, and had a mean test weight (TW) of 72.2 kg/hl. The SID of CP in the barley genotypes varied from 69% to 74%, and was greater ( P < 0.01) for genotypes Travira, Anisette and Metaxa compared to Yool and Campanile. Standardized ileal digestibility of Lys, Met and Trp ( P < 0.05) but not of Thr differed between genotypes. Moreover, barley genotypes differed in their standardized ileal digestible content (cSID) of CP and AA. Furthermore, SID and cSID of CP and most AA linearly decreased ( P < 0.05) with increasing NDF and total sugar content. Standardized ileal digestibility of CP and some AA and cSID of CP and most AA decreased linearly with increasing TW ( P < 0.05). Additionally, SID and cSID of CP and AA of most barley genotypes were lower when compared to tabulated values. In conclusion, a comprehensive database on chemical composition and SID of CP and AA in eight current barley genotypes has been made available. However, as present SID values are lower compared to feed tables, adjustments are required to minimize the risk of overestimating the actual protein value of barley for pigs.

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“…2). The apparent MW by SDS-PAGE was ca 14500 for both proteins, but it should be pointed out that some proteins with hydrophobic domains are known to deviate from the mobility in SDS-PAGE that would correspond to their MW [11,12]. …”

Section: Solubility Properties and Purificationmentioning

confidence: 97%

Lipid binding proteins from the endosperms of wheat and Oats

et al. 1984

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Abstract-A protein, designated lipid binding protein (LBP), has been purified from the petrol extracts of wheat and oat endosperms by hydrochloric acid precipitation in a non-polar médium and preparative electrophoresis. The purified LBP appeared to be homogeneous both by electrophoresis in sodium dodecyl sulphate-polyacrylamide (SDS-PAGE) gels (MW ca 14 500) and by electrophoresis (PAGE) at pH 3.2. The amino acid composition indicates a high degree of homology between the LBPs from the two sources, as judged by the indexes of Cornish-Bowden and of Harris and Teller. As in the case of thionin, a previously characterized polypeptide from the ether extract, LBP becomes etherinsoluble, chloroform-soluble by precipitation with acetone, and solubility in ether is restored by binding of digalactosyl diglyceride to the chloroform-soluble form.

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The Extraction, Solubility, and Characterization of Two Groups of Barley Storage Polypeptides

Cited by 112 publications

References 1 publication

The prolamin storage proteins of cereal seeds: structure and evolution

The prolamin storage proteins of cereal seeds: structure and evolution

Standardized ileal digestibility of amino acids in eight genotypes of barley fed to growing pigs

Lipid binding proteins from the endosperms of wheat and Oats

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