Seed Proteins

Brohult, Sven; Sandegren, E.

doi:10.1016/b978-0-12-395722-1.50011-2

Cited by 29 publications

(16 citation statements)

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“…The prolamin fractions of the various cereals have been given names: gliadin (wheat), secalin (rye), hordein (barley) and avenin (oats). Avenin makes up for only 10 -15% of the total protein, whereas gliadin, hordein and secalin account for 35 -50% (Brohult & Sandegren, 1954). It has been argued that the apparently non-toxic nature of oats may be due to the presence of a low percentage of oat prolamin, or more important, the different amino acid composition in oats compared with wheat.…”

Section: Discussionmentioning

confidence: 99%

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Adult coeliac patients do tolerate large amounts of oats

et al. 2003

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Objective: The aim of the present study was to investigate whether adult patients with coeliac disease in remission could include large amounts of oats in their daily gluten-free diet for an extended period of time without adverse effects. Design, subjects and methods: Twenty adult coeliac patients in remission included large amounts of uncontaminated rolled oats in their daily diet for a prolonged period. The examinations, performed four times during the study period, included small bowel endoscopy with biopsies, blood samples (nutritional status, serological analysis), height and body weight, gastrointestinal symptoms and dietary records. Gastrointestinal symptoms and diet were also investigated through unannounced telephone interviews once a month during the study period. Results: No adverse effects of a large intake of oats were seen in small bowel histology, serology nor in nutritional status in the 15 subjects who completed the whole study period. Two of the subjects dropped out because of gastrointestinal symptoms and three for non-medical reasons. The median intake of oats was 93 g=day and the compliance to the oat diet was found to be good. Examinations of the patients after drop-out did not show any deterioration in small bowel histology or nutritional status nor raised levels of antibodies. Conclusion: Results from this study indicate that adult patients with coeliac disease in remission can include large amounts of controlled wheat-free rolled oats for an extended period of time without adverse effects.

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Section: Discussionmentioning

confidence: 99%

“…As the amount of prolamine, the potentially toxic protein fraction in oats, is small compared with wheat, rye and barley (Brohult & Sandegren, 1954), it has been argued that oats given in large quantities may still be toxic in patients with coeliac disease.…”

Section: Introductionmentioning

confidence: 99%

Adult coeliac patients do tolerate large amounts of oats

et al. 2003

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“…The globulin fraction accounts for the majority of total seed protein (1,13,14). The alcohol-soluble prolamin fraction, which is the major seed storage protein in most cereals, is very low in oats (1,6,11,13,14).In To determine the solubility of oat globulin under various conditions, the defatted flour was extracted with 1 M NaCl, 0.05 M Tris (pH 8.5) at a ratio of 100 ml/g, using magnetic stirring at room temperature for 1 to 2 hr. The extract was centrifuged for 20 min at 23 C and 27,000g, and the supernatant was dialyzed against two changes of distilled H20 at 4 C, precipitating the globulin.…”

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confidence: 99%

“…In oat (Avena sativa L.) kernels, the primary storage protein is classified as a globulin because of its solubility in dilute salt solution but insolubility in water (1). The globulin fraction accounts for the majority of total seed protein (1,13,14).…”

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Subunit Structure and Composition of Oat Seed Globulin

Peterson¹

1978

Plant Physiol.

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Oat (Avena sadva L.) seed globuln was extracted from pound caryopses with 1 M NaCI, 0.05 M Tris(hydroxymethyl)antnoethane (pH 8.5) at room temperature. The globulin had a sedimentation constant of 12.1, and a molecular weight of 322,000, as determined by analytical ultracentrifugation. The globulin could be separated into two major subunits by sodiumdodecyl sulfate polyacrylamide gel electropboresis. Molecular weights of the subunits were 21,700 (a) and 31,700 (p8), and they were present in equimolar amounts. A subunit model of 6a and 6p8 per molecule of globulin is proposed. Amino acid analysis ilndicated that the a subunit contained more basic amino acids and aspartic acid/asparagine but less glutamic acid/glutamine and glycine than the p subunit.In oat (Avena sativa L.) kernels, the primary storage protein is classified as a globulin because of its solubility in dilute salt solution but insolubility in water (1). The globulin fraction accounts for the majority of total seed protein (1,13,14). The alcohol-soluble prolamin fraction, which is the major seed storage protein in most cereals, is very low in oats (1,6,11,13,14).In To determine the solubility of oat globulin under various conditions, the defatted flour was extracted with 1 M NaCl, 0.05 M Tris (pH 8.5) at a ratio of 100 ml/g, using magnetic stirring at room temperature for 1 to 2 hr. The extract was centrifuged for 20 min at 23 C and 27,000g, and the supernatant was dialyzed against two changes of distilled H20 at 4 C, precipitating the globulin. Ten-ml aliquots of the dialysate were centrifuged as above, but at 1 C to collect the suspended globulin precipitate. The various test solutions (1.5 ml) were added, and a Vortex mixer and ultrasonic bath were used at 23 C to achieve maximum dissolution. The solutions were centrifuged at 23 C and 27,000g for 20 min to pellet the undissolved protein, and the supernatants were assayed for protein (9) using BSA (Sigma, fraction V) as the standard.The globulin was normally prepared by extraction and dialysis as described above, and the dialysate was freeze-dried to recover the globulin from suspension. The dried globulin was stored indefinitely at -20 C.Analytical Ultracentrifugation. The oat globulin was dissolved in 0.5 M NaCl, 0.05 M Tris (pH 8.5) at a concentration of 3.2 mg/ml for sedimentation velocity analysis at 40,000 rpm and 20C on a Spinco model E ultracentrifuge. S20, was determined as described by Svedberg and Pedersen (18). For mol wt estimation, a sedimentation equilibrium analysis was done at 10,589 rpm, 20 C, for 10 hr. Partial specific volume was estimated by summation of the products of partial specific volume and weight per cent of each amino acid (16). Mol Wt Estimation by Polyacrylamide Gel Electropboresis. Oat globulin was solubilized in Triton X-100 and electrophoresed on polyacrylamide gels containing 4 to 10% acrylamide. The procedures of Hearing et al. (7)

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The Biosynthesis of Dicarboxylic Amino Acids and Enzymic Transformations of Amides in Plants

Wl¹

1959

Advances in Enzymology - And Related Areas of Molecular Biology

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Seed Proteins

Cited by 29 publications

References 78 publications

Adult coeliac patients do tolerate large amounts of oats

Adult coeliac patients do tolerate large amounts of oats

Subunit Structure and Composition of Oat Seed Globulin

The Biosynthesis of Dicarboxylic Amino Acids and Enzymic Transformations of Amides in Plants

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