Isolation and characterisation of A wheat albumin

Ewart, J. A. D.

doi:10.1002/jsfa.2740201208

Cited by 14 publications

(2 citation statements)

References 19 publications

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“…Protein S, lacking one arginine residue, was readily distinguished from the other proteins. CNBr cleavage gave four major peptides from each protein, as expected from the knowledge that these proteins each consist of a single chain (Ewart, 1969(Ewart, , 1972Silano et al 1973) and contain three methionine residues. The similarity of equivalent peptides ( Fig.…”

Section: Discussionsupporting

confidence: 56%

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

Redman¹

1975

Biochemical Journal

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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.

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Section: Discussionsupporting

confidence: 56%

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

Redman¹

1975

Biochemical Journal

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“…Since then several workers have studied the a-amylase inhibitors in wheat (Shainkin and Birk 1970;Silano et al 1973; Saunders and Lang 1973;Petrucci et al 1974Petrucci et al ,1975Buonocore et al 1976;De Ponte et al 1976). Earlier, others had worked on the same wheat albumins without knowing that they had the ability t o inhibit a-amylase (Nimmo et al 1963; Fish and Abbott 1969;Ewert 1969; Feillet and Nimmo 1970;Sodini et al 1970; Cantagalli et al 1971). Shainkin and Birk (1970) purified and characterized two different a-amylase inhibitors.…”

Section: Introductionmentioning

confidence: 99%

Purification and Characterization of ?-Amylase Inhibitors in Wheat (Triticum Aestivum Var. Anza)

Granum¹,

Whitaker

1978

J Food Biochemistry

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Three α‐amylase inhibitors were purified to homogeneity from Anza wheat (Triticum aestivum var. Anza) by extraction with 70% ethanol, ammonium sulfate fractionation and column chromatography on DEAE‐cellulose, CM‐ceillulose and Sephadex G‐50. Homogeneity was determined by disc gel and isoelectric focusing electrophoresis and by sedimentation equilibrium centrifugation. The inhibitors are designated 0.19, 0.28 and 0.55 on basis of their relative electrophoretic mobilities on polyacrylamide gels. The 0.19, 0.28 and 0.55 inhibitors had molecular weights of 24,000, 18,500 and 30,000 by polyacrylamide gel electrophoresis with different gel concentrations while the former two were 29,000 and 14,500 by sedimentation equilibrium centrifugation, respectively. The molecular weight of the 0.55 inhibitor was not determined by centrifugation. The isoelectric points were 5.9, 5.2 and 4.2 for the 0.19, 0.28 and 0.55 inhibitors, respectively. The three inhibitors had similar amino acid compositions but differed significantly in amounts of lysine, arginine, histidine, alanine, valine and phenylalanine. The 0.19 inhibitor was active against human salivary and hog pancreatic α‐amylases but inactive against Bacillus subtilis and Aspergillus oryzae α‐amylases. The 0.28 inhibitor had very weak activity against only human salivary α‐amylase. The 0.55 inhibitor had activity against only human salivary α‐amylase. The 0.55 inhibitor appears to differ from all previously reported wheat α‐amylase inhibitors while the 0.28 inhibitor (protein) is unique in having essentially no inhibitory activity.

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Relationship between wheat proteins

Booth¹,

Ewart²

1970

J Sci Food Agric

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Recent evidence including amino acid analyses, immunological tests and fingerprinting suggests that the gliadins of wheat varieties have evolved from a common ancestral protein by a series of mutations. No evidence to support a relationship of this nature between the gliadin, albumin and globulin classes was found. Confirmation of the genetic link between wheat and barley is provided by the close structural affinity between purothionin and its barley counterpart. There are some similarities in amino acid composition between a barley trypsin inhibitor and a wheat albumin. Available evidence, though scanty, is significant enough to justify the generalisation that storage proteins of identical mobility in different wheat varieties have closely similar primary and tertiary structures. Although the individual gliadins within a given variety are mutationally linked, their tertiary structures as judged by immunological tests show characteristic differences.

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Isolation and characterisation of A wheat albumin

Cited by 14 publications

References 19 publications

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

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

Purification and Characterization of ?-Amylase Inhibitors in Wheat (Triticum Aestivum Var. Anza)

Relationship between wheat proteins

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