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Peptide B 3142, which has been isolated from a peptic tryptic digest of whole gliadin by several separation steps [1], was examined for coeliac activity in an immunological test and in an organ-culture test, comparing enlarged groups of coeliac patients and control persons. In both test systems the peptide shows a coeliac specific effect. The N-terminal(More)
Larger amounts of coeliac active peptides are required for pathogenetic investigations. Therefore, a simplified preparative procedure by means of gel-permeation chromatography and reversed-phase HPLC was developed for the isolation of the peptides B3141-B3146, which are present in peptic tryptic digests of gliadin [this journal (1983) 176:85-94]. The(More)
Two Cheddar cheeses from two different production plants were ripened over 24 weeks at 10 degrees C and then analysed for peptides soluble in citrate buffer at pH 4.6 by reversed-phase (RP)-HPLC. Thirteen peptides with a chain length of between 35 and 65 amino acid residues and molecular masses between 3800 and 7400 were isolated and assigned to the(More)
The coeliac active peptide B 3142, which has been isolated from a peptic-tryptic digest of gliadin and which consists of 53 amino-acid sequences, was partially hydrolyzed with alpha-chymotrypsin. The two fragment peptides CT-1 (positions 1-22 of B 3142) and CT-2 (positions 23-53) were separated by high-performance liquid chromatography on octadecyl silica(More)
Ten potato varieties, with different rates of browning, were analyzed quantitatively for phenoloxidase, tyrosine, chlorogenic acid, caffeic acid, and for reducing substances (ascorbic acid). The rate of tyrosine turnover was calculated from the data. The fact that the further reactions of the primary oxidation products leading to browning only take place(More)
beta-Casein A2 was isolated from milk of a homozygous cow and hydrolysed with trypsin. The hydrolysate was separated by RP-HPLC into 18 peptides, all but one of which could be attributed to the sequence of beta-casein on the basis of the amino acid composition. Some peptides overlapped. In total, they represented about 97% of the protein sequence. Only(More)
To determine the toxic effect of different gliadins on coeliac patients, which has been variably assessed in the literature, wheat prolamines (gliadin) were separated into the main fractions alpha-, beta-, gamma-, and omega-gliadins by chromatography on Sulfopropyl Sephadex C-50. The chemical compositions of the gliands were characterized by polyacrylamide(More)
Reduced glutenin is separated by gel permeation high-performance liquid chromatography into three major and five minor fractions, which significantly differ in their amino acid compositions. By reversed-phase high performance liquid chromatography, about 20 glutenin components are obtained. These can be classified into three groups according to their amino(More)
For the isolation of coeliac active peptide fractions the peptic tryptic digest of whole gliadin was successively separated by ultrafiltration, gel filtration, cation-exchange chromatography, anion exchange chromatography and high-performance liquid chromatography. After each separation step the peptide fractions obtained were characterized by amino acid(More)
Glutenin was prepared from gluten of the wheat variety Rektor by extraction of gliadin with aqueous ethanol. It was cleaved successively into soluble peptides by the enzymes trypsin and thermolysin. Separation of the peptide mixtures was performed by gel permeation chromatography (GPC) on Sephadex G25 and reversed phase high performance liquid(More)