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

ISOLATION OF 3 ANTIBACTERIAL PEPTIDES FROM PIG INTESTINE - GASTRIC-INHIBITORY POLYPEPTIDE(7-42), DIAZEPAM-BINDING INHIBITOR(32-86) AND A NOVEL FACTOR, PEPTIDE-3910
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DOI:
10.1111/j.1432-1033.1993.tb18182.x
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发表时间:
1993-09-01
期刊:
EUROPEAN JOURNAL OF BIOCHEMISTRY
影响因子:
--
通讯作者:
BOMAN, HG
BOMAN, HG
中科院分区:
其他
文献类型:
--
作者:
AGERBERTH, B;BOMAN, A;BOMAN, HG

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两种抗菌肽,cecropin P1和PR-39(39-残基脯氨酸/精氨酸丰富肽),此前已从猪小肠上部分离并鉴定。我们现在继续在肠道激素分离过程中产生的不同侧组分中寻找抗菌肽。从一个这样的片段开始,监测对巨型芽孢杆菌的活性,我们通过三个连续的色谱步骤分离出三个均质肽。氨基酸序列分析结合质谱分析确定了两种肽,分别为胃抑制多肽(7-42)[GIP(7-42)]和地西泮结合抑制剂(32-86)[DBI(32-86)],来源于已知的因素。然而,完整的GIP和DBI本身几乎没有任何抗菌活性。第三个肽构成了一个以前未知的结构,根据其分子质量被命名为肽3910。3种多肽均对巨芽孢杆菌具有良好的抑制活性。此外,GIP(7-42)对化脓性链球菌和外膜缺陷的大肠杆菌突变体有一定的活性。
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.