ISOLATION OF 3 ANTIBACTERIAL PEPTIDES FROM PIG INTESTINE - GASTRIC-INHIBITORY POLYPEPTIDE(7-42), DIAZEPAM-BINDING INHIBITOR(32-86) AND A NOVEL FACTOR, PEPTIDE-3910

被引:64
作者
AGERBERTH, B
BOMAN, A
ANDERSSON, M
JORNVALL, H
MUTT, V
BOMAN, HG
机构
[1] KAROLINSKA INST, DEPT CHEM 1, S-17177 STOCKHOLM, SWEDEN
[2] UNIV STOCKHOLM, DEPT MICROBIOL, S-10691 STOCKHOLM, SWEDEN
来源
EUROPEAN JOURNAL OF BIOCHEMISTRY | 1993年 / 216卷 / 02期
关键词
D O I
10.1111/j.1432-1033.1993.tb18182.x
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Two antibacterial peptides, cecropin P1 and PR-39 (39-residue proline/arginine-rich peptide), from the upper part of pig small intestine have previously been isolated and characterized. We have now continued our search for antibacterial peptides in different side fractions generated during the isolation of intestinal hormones. Starting from one such fraction and monitoring activity against Bacillus megaterium, we isolated three homogeneous peptides by three consecutive chromatographic steps. Amino acid sequence analysis in combination with mass spectrometry identified two of the peptides as gastric inhibitory polypeptide(7-42) [GIP(7-42)] and diazepam-binding inhibitor(32-86) [DBI(32-86)], derived from factors already known. However, intact GIP and DBI have hardly any antibacterial activity by themselves. The third peptide constitutes a previously unknown structure, designated as peptide 3910 from its molecular mass. All three peptides showed good activity against B. megaterium. In addition, GIP(7-42) showed some activity against Streptococcus pyogenes and an Escherichia coli mutant with a defect in its outer membrane.
引用
收藏
页码:623 / 629
页数:7
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