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Isolation of a low-molecular-weight antibacterial system from human amniotic fluid
Journal article   Open access   Peer reviewed

Isolation of a low-molecular-weight antibacterial system from human amniotic fluid

Patrick Schlievert, William Johnson and Rudolph P Galask
Infection and immunity, Vol.14(5), pp.1156-1166
11/1976
DOI: 10.1128/IAI.14.5.1156-1166.1976
PMCID: PMC415508
PMID: 789241
url
https://doi.org/10.1128/IAI.14.5.1156-1166.1976View
Published (Version of record) Open Access

Abstract

A low-molecular-weight antibacterial system has been isolated from human amniotic fluid. The bacterial inhibitor requires the metal cation zinc and a peptide with a molecular weight of 630. The peptide component was purified using ultrafiltration, gel filtration, and ion-exchange chromatography. It can be inactivated by digestion with carboxypeptidase. The amino acid composition of the peptide is: 3 glutamine-glutamic acid, 2 glycine, and 1 lysine. Removal of zinc from the peptide has been shown to remove bacterial inhibitory activity.
Chromatography, Ion Exchange Molecular Weight Ultrafiltration Carboxypeptidases - pharmacology Culture Media Dithizone - pharmacology Electrophoresis, Polyacrylamide Gel Humans Amniotic Fluid - microbiology Escherichia coli - growth & development Zinc - pharmacology Chromatography, Gel

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