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At least 109 records · Page 6Linked to original sources
PubMed2003

Development of a monoclonal antibody capable of detecting prolamine in wheat and oats.

A monoclonal antibody (MAb) capable of detecting the gliadin in wheat flour has been developed. By immunoblot, the monoclonal antibody recognized three bands in the membranes after electrophoresis in an SDS PAGE of the alcohol-soluble proteins of wheat, and only one band in the alcohol extract of the oat flour. ELISA technique can be applied using this monoclonal antibody in the detection of gliadin and avenin in samples from wheat or triticale. The characterization of the antibody shows that it is an IgM class. Sensitivity by ELISA to the gliadin was 80 ng/ml.

Alcohols↗
PubMed1997

The wheat transcriptional activator SPA: a seed-specific bZIP protein that recognizes the GCN4-like motif in the bifactorial endosperm box of prolamin genes.

The conserved bifactorial endosperm box found in the promoter of wheat storage protein genes comprises two different cis elements that are thought to be involved in regulating endosperm-specific gene expression. Endosperm nuclear extracts contain binding activities. One is called ESBF-I, which binds to the endosperm motif (EM), and the other is called ESBF-II, which binds to the GCN4-like motif(GLM). Here, we present a functional analysis of the endosperm box of a low-molecular-weight glutenin gene found on the 1D1 chromosome of hexaploid wheat (LMWG-1D1) in transgenic tobacco plants. Our analysis demonstrates the necessity of the EM and GLM for endosperm-specific gene expression and suggests the presence in tobacco of functional counterparts of wheat ESBF-I and ESBF-II. Furthermore, we describe the isolation and characterization of cDNA clones encoding SPA, a seed-specific basic leucine zipper protein from wheat that can activate transcription from the GLMs of the -326-bp LMWG-1D1 promoter in both maize and tobacco leaf protoplasts. This activation is also partially dependent on the presence of functional EMs, suggesting interactions between SPA with ESBF-I-like activities.

Amino Acid Sequence↗
PubMed2002

Molecular cloning, sequencing, and chromosome mapping of a 1A-encoded omega-type prolamin sequence from wheat.

Gliadins are the most abundant component of the seed storage proteins in cereals and, in combination with glutenins, are important for the bread-making quality of wheat. They are divided into four subfamilies, the alpha-, beta-, gamma-, and omega-gliadins, depending on their electrophoresis pattern, chromosomal location, and DNA and protein structures. Using a PCR-based strategy we isolated and sequenced an omega-gliadin sequence. We also determined the chromosomal subarm location of this sequence using wheat aneuploids and deletion lines. The gene is 1858 bp long and contains a coding sequence 1248 bp in length. Like all other gliadin gene families characterized in cereals, the omega-gliadin gene described here had characteristic features including two repeated sequences 300 bp upstream of the start codon. At the DNA level, the gene had a high degree of similarity to the omega-secalin and C-hordein genes of rye and barley, but exhibited much less homology to the alpha- and beta-gliadin gene families. In terms of the deduced amino acid sequence, this gene has about 80 and 70% similarity to the omega-secalin and C-hordein genes, respectively, and possesses all the features reported for other gliadin gene families. The omega-gliadin gene has about 30 repeats of the core consensus sequences PQQPX and XQQPQQX, twice as many as other gliadin gene families. Southern blotting and PCR analysis with aneuploid and deletion lines for the short arm of chromosome 1A showed that the omega-gliadin was located on the distal 25% of the short arm of chromosome 1A. By comparison of PCR and A-PAGE profiles for deletion stocks, its genomic location must be at a different locus from gli-Ala in 'Chinese Spring'.

Amino Acid Sequence↗
PubMedDate not supplied

The determination of prolamins in gluten-free food. Introductory remarks.

This paper gives the considerations on the Codex Alimentarius Standard on gluten free food and the levels that are proposed as a new standard. Background for the level of tolerance for gliadin in coeliac patients is given as well as the arguments for the choice of an enzyme immunochemical method for the determination of gliadin in gluten free food.

Dietary Proteins↗
PubMedDate not supplied

Chemistry, coeliac-toxicity and detection of gluten and related prolamins in foods.

Some recent advances in the understanding of the chemistry of gluten proteins and its relationship to the toxicity of different fractions in coeliac disease (gluten intolerance) is reviewed. Most recent studies on gluten toxicity have used in vitro analyses of cellular immune activation by gluten fractions and peptides. Our work indicates that gliadin is the most active of the different protein families found within the wheat grain and that a specific peptide sequence located in the amino terminus domain of alpha-gliadin and containing the sequence proline-serine-glutamine-glutamine was most active. Improvement in the dietary management of coeliac disease is possible by use of test kits for the detection of gluten in foods. Both laboratory kits and home test kits (suitable for use by individual coeliacs) are available and reliably detect gluten from wheat, rye and barley even after cooking or baking.

Celiac Disease↗