CELIAC ACTIVE PEPTIDES FROM GLIADIN - LARGE-SCALE PREPARATION AND CHARACTERIZATION

被引：9

作者：

WIESER, H ^{[1
]}

BELITZ, HD ^{[1
]}

机构：

[1] TECH UNIV MUNICH,INST LEBENSMITTELCHEM,W-8046 GARCHING,GERMANY

来源：

ZEITSCHRIFT FUR LEBENSMITTEL-UNTERSUCHUNG UND-FORSCHUNG | 1992年 / 194卷 / 03期

关键词：

D O I：

10.1007/BF01198412

中图分类号：

TS2 [食品工业];

学科分类号：

0832 ;

摘要：

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 peptides: are derived from the N-terminal part of alpha-gliadins and are closely related. The amino acid sequence of B3143 is VPVPQLQPQNPSQQQPQEQVPLVQQQQFPGQQQQFPPQQPYPQPQPFPSQQPYL. B3144 has proline instead of glutamine in position 34. The previously described peptide B3142 [this journal (1984) 179:371-376] corresponds to B3144 except for the missing C-terminal leucine.

引用

页码：229 / 234

页数：6

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