SEARCH · PubMed Health

Results for “Prolamins”

Explore indexed PubMed citations for clinical trials, systematic reviews and public health research. Read source abstracts and follow each citation to its original PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 73 records · Page 4Linked to original sources

PubMed1990

Detection and estimation of the barley prolamin content of beer and malt to assess their suitability for patients with coeliac disease.

Malt, lager, brown ale, bitter and stout were assessed for their barley prolamin (hordein) content. Monoclonal antibody immunoperoxidase staining of electrophoretically separated samples of beer revealed the presence of immunoreactive hordein. Polyclonal antibody based enzyme linked immunosorbant assays (ELISAs) revealed 1.6 mg of hordein per gram of malt and 1.5 mg per pint in the beers. Patients with coeliac disease should avoid ingestion of beer and foods that contain malt since they contain quantifiable amounts of hordein that is known to exacerbate the condition.

Alkaline Phosphatase↗

PubMed1997

A small peptide from durum wheat gliadin prevents cell agglutination induced by prolamin-peptides toxic in coeliac disease.

A peptide (m.w. 1157.5 Da) able to prevent the agglutination of K562(S) cells induced by the peptic-tryptic prolamine digests of the cereals toxic in coeliac disease (i.e. bread wheat, rye, barley and oat) was characterized as one of the components of the peptic-tryptic digest of durum wheat gliadin. This peptide was synthesized in a high degree of purity with the solid phase method with the Applied Biosystem 431A. An amino acid sequence was identified in the 1157.5 Da peptide as being related to the largest common sequences previously detected in a series of bread wheat toxic peptides by other authors.

Agglutination↗

PubMed2004

Interaction of two prolamins with 1-13C oleic acid by 13C NMR.

In this paper, we analyzed the interaction of Z19 prolamin from a BR451 maize variety and pennisetin from a BRS1501 pearl millet variety with 1-(13)C-enriched oleic acid (OA) by (13)C NMR in solution. In both proteins, we identified the presence of free fatty acids by NMR in solid state and solution. The interactions were analyzed at the protein/OA molar ratios of 1:1 and 1:4. In the Z19/OA 1:1 mixture in 70% ethanol and 30% D(2)O, the chemical shift of OA C1 was 182.9 ppm, about 3 ppm above that of the pure OA in the same solvent. In contrast, upon addition of OA to the pennisetin (1:1), the chemical-shift value slightly decreased by less than 1 ppm. The chemical-shift titration curve of OA C1 in an apparent pH range of 5.5-7.3 shifted by approximately 0.3 pH units toward higher pH values in the pennisetin/OA 1:1 complex relative to the pure OA. The results obtained for the pennisetin/OA 1:4 mixture were similar to the complexes at a 1:1 molar ratio. A significant difference was observed between the 1:1 and 1:4 curves for Z19. The titration curve for Z19/OA 1:1 suggested specific binding at the sites with electrostatic interaction.

Carbon Isotopes↗

PubMed1993

A role for gamma 3 hordein in the transport and targeting of prolamin polypeptides to the vacuole of developing barley endosperm.

Hordein synthesis, transport and deposition was analysed by immunocytochemistry in developing endosperm cells of wild-type (Carlsberg II) and mutant varieties deficient in B hordein (hor2ca), gamma 1 hordein (Donetsky), gamma 2 hordein and minor B hordein polypeptides (Haisa), or gamma 3 hordein (Nevsky). In all varieties, hordein polypeptides were detected both in the cytoplasm as globules, ranging in diameter from 50 nm to 1.24 microns, and in the vacuole as protein bodies. In the cytoplasmic globules B and C hordein polypeptides are assembled as a core and are surrounded by an outer layer of gamma 1 and gamma 2 hordein. The globules apparently fuse several times in the cytoplasm before entering the vacuole. Absence of gamma 3 hordein in the mutant Nevsky leads to a dramatic change in hordein polypeptide targeting, the hordein storage proteins being largely deposited in the lumen of the rough endoplasmic reticulum. gamma 3 Hordein is unique among the sulphur-rich hordein polypeptides, being monomeric and forming only intramolecular disulphide bridges, while the other B and gamma hordein polypeptides are aggregated by intermolecular disulphide bridges. Retention of hordein in the rough endoplasmatic reticulum in the absence of gamma 3 hordein suggests that gamma 3 hordein may maintain the prolamin storage polypeptides in a transport competent state. The sequence of the mature gamma 3 hordein polypeptide was deduced from a cDNA clone, and compared with gamma 2 hordein. The epitope recognized by the gamma 1 + gamma 2 hordein-specific BX monoclonal antibody used for immunocytochemistry was mapped to include E190 and K193, by synthesizing overlapping oligopeptides.

Amino Acid Sequence↗

PubMed1998

An endosperm-specific DOF protein from barley, highly conserved in wheat, binds to and activates transcription from the prolamin-box of a native B-hordein promoter in barley endosperm.

A cDNA encoding a DNA-binding protein of the DOF class of transcription factors was isolated from a barley endosperm library. The deduced amino acid sequence for the corresponding protein is 94% identical through the DOF domain to the prolamin-box (P-box) binding factor PBF from maize. The gene encoding the barley PBF (BPBF) maps to chromosome 7H, and its expression is restricted to the endosperm where it precedes that of the hordein genes. The BPBF expressed in bacteria as a GST-fusion binds a P-box 5'-TGTAAAG-3' containing oligonucleotide derived from the promoter region of an Hor2 gene. Binding was prevented when the P-box motif was mutated to 5'-TGTAgAc-3'. A P-box binding activity, present in barley and wheat endosperm nuclei, interacted similarly to BPBF with this synthetic oligonucleotide, and the binding was abolished by 1,10-phenanthroline. Transient expression experiments in developing barley endosperms demonstrate that BPBF transactivates transcription from the P-box element of a native Hor2 promoter and that direct binding of BPBF to its target site is essential for transactivation since mutations in the DOF DNA-binding domain or in the P-box motif of this promoter abolished both binding and transactivation. Evidence was also obtained for the presence in wheat of a Pbf homologue having similar DNA-binding properties to that of BPBF. These results strongly implicate this endosperm-specific DOF protein from barley as an important activator of hordein gene expression and suggest the evolutionary conservation of the Pbf gene function among small grain cereals.

Amino Acid Sequence↗

PubMed1994

The transcriptional activator Opaque2 recognizes two different target sequences in the 22-kD-like alpha-prolamin genes.

The maize Opaque2 (O2) protein is a "leucine zipper" DNA binding factor that interacts with the sequence TCCACGTAGA in the promoters of the 22-kD alpha-zein genes and activates its transcription. A completely different consensus sequence (GATGAPyPuTGPu) identified in b-32, a gene that encodes an abundant albumin that is also under control of the O2 locus, can also be bound by the O2 protein. We showed that the gene encoding the 22-kD-like alpha-coixin, the alpha-prolamin of the maize-related grass Coix, can also be transactivated by the O2 protein. A binding assay in vitro and footprint analysis demonstrated that the GACATGTC sequence of the alpha-coixin promoter can be recognized and protected by the maize O2 protein. Employing transient expression experiments in immature maize endosperm and tobacco mesophyll protoplasts, we demonstrated that the O2 protein can activate expression of the beta-glucuronidase reporter gene placed under the control of the 22-kD-like alpha-coixin promoter. We also demonstrated that a 22-kD-like alpha-coixin pseudogene promoter is transactivated by the maize O2 protein.

Base Sequence↗

PubMed1999

Geographical variation of the alleles at the two prolamin loci, Pro1 and Pro2, in foxtail millet, Setaria italica (L.) P. Beauv.

Allelic variation at the two prolamin loci (Pro1 and Pro2) and its geographical distribution in 560 local cultivars of foxtail millet (Setaria italica) mainly from Eurasia were studied using SDS-polyacrylamide gel electrophoresis (SDS-PAGE). Genetic analysis of a newly detected polymorphic band, band 6, indicated that it is controlled by an allele at the Pro2 locus, which was designated as Pro2f. Two alleles (Pro1a and Pro1null) at the Pro1 locus and six alleles (Pro2a, Pro2b, Pro2c, Pro2d, Pro2e and Pro2f) at the Pro2 locus were detected among the cultivars examined. Although the frequency of the Pro1a allele varied from 0% in the Nansei islands of Japan and Africa to 66% in Afghanistan, no apparent trend was observed in geographical distribution. In contrast, two common alleles at the Pro2 locus, Pro2b and Pro2f, had clear differential geographical distribution. The Pro2b allele was most frequent in Europe and decreased in frequency eastwards. The Pro2f allele occurred frequently in subtropical and tropical regions including the Nansei islands of Japan, the Philippines, Nepal, India, Pakistan and Africa. All eight alleles at the Pro1 and Pro2 loci occurred in China, suggesting China is a center of diversity. The origin of geographical differentiation of local cultivars into a "tropical group" characterized by the Pro2f allele and other genes was discussed.

Africa↗

PubMed1996

Cloning and sequencing of a rice gene encoding the 13-kDa prolamin polypeptide.

A gene encoding the 13-kDa prolamin polypeptide was isolated from a rice genomic library (lambdaEMBL3) and the nucleotide sequence of an about 3-kbp EcoRI fragment was analyzed. The cloned gene (NRP33) codes for a protein composed of 156 amino acids, including a signal peptide of 19 amino acid residues and no intron is present in the genomic clone. The nucleotide sequence contains consensus TATA and CAAT boxes, and two polyadenylation signals. In addition, there are two conserved sequences named the -- 300 element and 10 consecutive repeats of the trinucleotide ATT in the 5' noncoding sequence.

Amino Acid Sequence↗

PubMedDate not supplied

[The carbohydrate components of corn prolamins].

This work was aimed to study the patterns of zein glycosylation. Zein proteins included 1-3% of sugars. The affinity of different lectins, such as concanavalin A (Con A), Lens culinaris lectin (LCL) and lectins of Arachis hypogaea (PNA), of Triticum vulgaris (WGA), of Dolichos biflorus (DBA), of Glycin max (SBA), of Lotus tetragonolobus (LTA), of Laburnum anagiroides (LAL), of Ricinus communis (RCA), of Phaseolus vulgaris (PHA) was used to analyze the glycosylation sites. All selected lectins interacted with zein proteins. It may serve a basis for determination of mannose, galactose, fucose and aminosugars. Some lectins were bound only by prolamines of some inbred lines, while others were connected with all lines.

Carbohydrate Metabolism↗

PubMed1990

Variation in the nucleotide sequence of a prolamin gene family in wild rice.

Variation in the DNA sequence of the 10 kDa prolamin gene family within the wild rice species Oryza rufipogon was probed using the direct sequencing of PCR-amplified genes. A comparison of the nucleotide and deduced amino-acid sequences of eight Asian strains of O. rufipogon and one strain of the related African species O. longistaminata is presented.

Amino Acid Sequence↗

PubMed1991

Long-term results in pancreatic transplantation with special emphasis on the use of prolamine.

Our pancreatic transplantation programme was initiated in 1979. Since then a total of 102 pancreas transplantations have been performed, blocking exocrine secretion using the duct occlusion technique with prolamine. Early non-immunological complications are frequent. The long-term results (9 years) in combined pancreas and kidney transplanted patients are satisfying: the survival rate for pancreas is 38% and 54% for kidney. Patient survival rate in this period is 85%. Beyond the first year post-transplant the exocrine activity disappears whereas the endocrine function remains well preserved.

Diabetes Mellitus, Type 1↗

PubMed1994

Chemical, nutritional and technological characteristics of buckwheat and non-prolamine buckwheat flours in comparison of wheat flour.

Chemical, nutritional, and technological characteristics of buckwheat and non-prolamine buckwheat flours in comparison to wheat for celiac patients use have been studied. The results suggested the following conclusions: the 56.5% extraction value for flour obtention is considered good; the buckwheat flour presents methionine and cystine as first limiting amino acids followed by threonine as the second limiting amino acid; the buckwheat flour presents higher content of lysine amino acids than the wheat flour; the buckwheat flour is superior to the wheat flour regarding iron, copper, and magnesium minerals; the buckwheat flour does not present haemagglutinin activity and the tannin content is negligible. Rheological assays indicate that the buckwheat flour does not contain gluten.

Brazil↗

PubMed2002

Sequence variation in the gene encoding the 10-kDa prolamin in Oryza (Poaceae). I. Phylogenetic Implications.

Oryza L. (Poaceae) contains approximately 20 wild and two domesticated species and nine genomes. Major disagreements exist on its systematics and genome evolution. Sequence polymorphism in the gene that encodes the 10-kDa prolamin polypeptide (a seed storage protein) was used to determine phylogenetic relationships and evaluate current systematics for 19 Oryza species. This gene in Oryza is approximately 402-bp long, and includes a 72-bp signal peptide region. A strict consensus tree shows Oryza brachyantha (FF) as the most basal species, followed by a polytomy of three clades that can be delineated based on genome composition: (1) the GG clade: Oryza granulata and Oryza meyeriana, (2) the EE clade: Oryza australiensis, and (3) the ABCD clade: the remaining Oryza species. Two subclades within the ABCD clade emerge, one containing species with the AA genome, the other with components of the BC and D genomes. Members of the AA subclade form a polytomy and were delineated by a single 3-base deletion. The African species Oryza punctata (BB) and the South American-endemic CCDD genome species form a strong lineage, pointing to a close genetic affinity of O. punctata to the missing DD genome donor. The strong association between the CC and BBCC species implies convergence at the gene level. The study supports the following sectional units of Oryza: Section Oryza (Series sativae and officinaliae), Section australiensis, Section Granulata, Section Brachyantha.

Journal Article↗

PubMed1998

Characterization of the maize prolamin box-binding factor-1 (PBF-1) and its role in the developmental regulation of the zein multigene family.

A maize prolamin box (P-box)-binding factor (PBF-1) has been purified and characterized from immature endosperm tissue. PBF-1 has a molecular weight of 38kDa. It is detected only in endosperm, but not in root or leaf tissues, consistent with its tissue-specific function. Site-directed mutagenesis experiments reveal that both the P-box and its flanking sequences are important for PBF-1 DNA binding. Developmental studies show that PBF-1 accumulates in the endosperm from 8 to at least 30days after pollination (DAP). From 16 to 24DAP, however, multiple shifted bands of protein(s)-DNA complexes can be observed, which correlate with an increase in zein gene expression. PBF-1 can also bind to the P-box from '22-kDa' and '19-kDa' zein promoters, but at a lower affinity than to the '27-kDa' zein promoter. The effects of protein dephosphorylation and zinc ion chelators on PBF-1 DNA binding activity are also shown. A model is proposed where PBF-1 serves as a 'recruiter' of class-specific transcription factors like Opaque2 (O2).

Chromatography, Affinity↗

PubMed2004

Conformation of the Z19 prolamin by FTIR, NMR, and SAXS.

The alpha zein, the maize storage prolamin, is a mixture of several homologous polypeptides that shows two bands in SDS-PAGE, called Z19 and Z22. The conformation studies carried out by several authors in this mixture are conflicting. To elucidate these inconsistencies, we analyzed the conformation of the Z19 fraction, extracted from BR451 maize variety by Fourier transform infrared spectroscopy, nuclear magnetic resonance, and small-angle X-ray scattering. The infrared results show that Z19 has 46% of alpha helix and 22% of beta sheet. The fast N-H to N-D exchange measured by (1)H NMR spectroscopy showed that Z19 is not a compact structure. The scattering measurements indicated an extended structure with 12 by 130 A. With these data, we have modeled the Z19 structure as a hairpin, composed of helical, sheet, turns, and secondary structures, folded back on itself.

Magnetic Resonance Spectroscopy↗

PubMed1987

[Morphologic findings after intracerebral administration of an alcoholic prolamine solution].

Morphological studies were performed after intracerebral injection of Ethibloc (E.), an alcoholic prolamine solution, to prove the usefulness of E. as a drug depot in the local chemotherapy of brain gliomas. Organisation of E. starts 2-3 weeks after injection, but remains incomplete even 24 weeks later. This depot cannot be removed in case of diminished drug concentration because of the extremely close connection with the adjacent brain tissue. Further repeated injection of drug into the E. depot cannot reach the tumours periphery because of the surrounding glial scar and connective tissue.

Animals↗

PubMed2002

Characterization of pearl millet prolamins.

We report the physical-chemical characterization of the major alcohol-soluble proteins present in seeds of pearl millet (Pennisetum glaucum) by SDS-PAGE, bidimensional gel electrophoresis, MALDI-TOF/MS and RP-HPLC. We demonstrate the presence of three major prolamins, called A-, B- and C-pennisetin with mass values around 27, 22 and 12 kDa, respectively. We present partial amino acid sequences of these major proteins, which should allow the posterior isolation of the respective genes.

Amino Acid Sequence↗

PubMed1978

[Application of hydrophobic chromatography to the fractionation of wheat prolamins].

Hydrophobic chromatography is applied to the fractionation of wheat prolamins. Proteins are separated on "Phenyl Sepharose CL 4B" column. They are eluted by variations of pH and polarity of solvent. Components with the same electrophoretic mobility appear in several chromatographic fractions and gliadin groups, as indicated by Woychick classification, are heterogeneous. This method is excepted to give new information about interaction properties of gluten proteins.

Amino Acids↗