AGGLUTINATING ACTIVITY OF WHEAT GLIADIN PEPTIDE FRACTIONS IN CELIAC-DISEASE

被引:22
作者
DEVINCENZI, M [1 ]
DESSI, MR [1 ]
GIOVANNINI, C [1 ]
MAIALETTI, F [1 ]
MANCINI, E [1 ]
机构
[1] UNIV CAGLIARI,FAC PHARM,INST BIOCHEM,CAGLIARI,ITALY
关键词
MANNAN; GLIADIN PEPTIDES; N; N'-DIACETYLCHITOBIOSE; N'; N''-TRIACETYLCHITOTRIOSE; CELIAC DISEASE; BREAD WHEAT; DURUM WHEAT;
D O I
10.1016/0300-483X(94)02912-E
中图分类号
R9 [药学];
学科分类号
1007 ;
摘要
The K 562 (S) cell agglutinating activity of peptides obtained from in vitro digestion of bread wheat gliadins has been shown to be associated with a small fraction (coded as Fraction C), that can be easily separated by affinity chromatography of the whole digest on a sepharose 6-B-mannan or sepharose 6-B-oligomers of N-acetyl-glucosamine. Although the whole gliadin digests from 12 durum wheat varieties were unable to agglutinate K 562 (S) cells, all these digests were found to contain an active Fraction C. The lack of agglutinating activity of the whole durum wheat gliadin digests has been shown to be associated with the presence in these digests of another peptide fraction (coded as Fraction B) that is eluted much earlier from the sepharose 6-B-mannan column and is able to inhibit the cell agglutinating activity of Fraction C. Such an active Fraction B is not present in bread wheat gliadin peptides, although peptides with the same elution profile as Fraction B have been detected.
引用
收藏
页码:29 / 35
页数:7
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