Recent advances in the study of prolamin storage protein organization and function [PDF]
Prolamin storage proteins are the main repository for nitrogen in the endosperm of cereal seeds. These stable proteins accumulate at massive levels due to the high level expression from extensively duplicated genes in endoreduplicated cells.
David Richard Holding
doaj +5 more sources
The prolamin storage proteins of cereal seeds: structure and evolution [PDF]
With the exception of rice, the major cereals falls into two groups. The temperate cereals comprise barley, wheat, rye and oats, and the tropical cereals maize, sorghum and millets. Only the prolamins of wheat, barley and maize have been studied in detail at the molecular and physicochemical levels, and we will therefore focus on these.
P R, Shewry, A S, Tatham
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Wheat gluten, and related prolamin proteins in rye, barley and oats cause the immune-mediated gluten intolerance syndrome, coeliac disease. Foods labelled as gluten-free which can be safely consumed by coeliac patients, must not contain gluten above a ...
Matthew Daly +5 more
doaj +3 more sources
Immunochemical relationships of the prolamin storage proteins of barley, wheat, rye and oats
Abstract The antigenic relationships of the major prolamin storage proteins and low-molecular-weight alcohol-soluble proteins of barley, wheat and rye and the prolamins of oats are studied using polyclonal antisera raised against purified protein (or groups of proteins) and quantitative laser nephelometry. In addition, the specificity of a previously
Festenstein, G. N. +2 more
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Effects of Reduced Prolamin on Seed Storage Protein Composition and the Nutritional Quality of Rice [PDF]
Rice seed storage proteins accumulate in two types of protein body (PB-I and PB-II) that are nutrient sources for animals. PB-I is indigestible and negatively affects rice protein quality. To improve the nutritional value of rice seeds we are aiming to engineer the composition and accumulation of endogenous seed storage proteins.
Kim, Hyun-Jung +4 more
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The Transport of Prolamine RNAs to Prolamine Protein Bodies in Living Rice Endosperm Cells[W] [PDF]
AbstractRNAs that code for the major rice storage proteins are localized to specific subdomains of the cortical endoplasmic reticulum (ER) in developing endosperm. Prolamine RNAs are localized to the ER and delimit the prolamine intracisternal inclusion granules (PB-ER), whereas glutelin RNAs are targeted to the cisternal ER.
Shigeki, Hamada +7 more
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Oxidative protein folding: Selective pressure forprolaminevolution in rice [PDF]
During seed development, endosperm cells of highly productive cereals, including rice, synthesize disulfide-rich proteins in large amounts and deposit them into storage organelles. Disulfide bond formation involves electron transfer and generates H(2)O(2) as a by-product.
Onda, Yayoi, Kawagoe, Yasushi
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Celiac disease specific prolamin peptide content of wheat relatives and wild species determined by ELISA assays and bioinformatics analyses. [PDF]
Enzyme-linked immunosorbent assays (ELISAs) are widely used to determine gluten contamination in gluten-free and low gluten food samples. ELISA assays developed using monoclonal antibodies against known toxic peptides have an advantage in the ...
Gell, Gyöngyvér Mónika +5 more
core +3 more sources
Maize protein quality is determined by the composition of its endosperm proteins, which are classified as nutritionally poor zeins (prolamin and prolamin-like) and nutritionally rich non-zeins (albumin, globulin, glutelin-like, and glutelin).
Mehak Sethi +5 more
doaj +1 more source
Brachypodium distachyon as a model for defining the allergen potential of non-prolamin proteins. [PDF]
Epitope databases and the protein sequences of published plant genomes are suitable to identify some of the proteins causing food allergies and sensitivities. Brachypodium distachyon, a diploid wild grass with a sequenced genome and low prolamin content, is the closest relative of the allergen cereals, such as wheat or barley.
Juhász A +5 more
europepmc +5 more sources

