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Arch Biochem Biophys. 1992 May 15;295(1):5-12.

Purification and primary structure of pediocin PA-1 produced by Pediococcus acidilactici PAC-1.0.

Author information

1
Quest International, Sarasota, Florida 34243.

Abstract

The plasmid-encoded bacteriocin pediocin PA-1, produced by the gram-positive bacterium Pediococcus acidilactici strain PAC-1.0, was purified to homogeneity. The purified product exhibited antibacterial activity against several gram-positive bacterial strains, including the food pathogen Listeria monocytogenes. Pediocin PA-1 is a 4629-Da peptide with 44 amino acids and two disulfide bonds. The amino acid sequence and arrangement of the disulfide bonds were determined. Sequence data were used to calculate an isoelectric point of 10.0. The small and basic nature of PA-1 is comparable to several other bacteriocins produced by gram-positive bacteria. Reported sequences of other bacteriocins and of other antimicrobial peptides from diverse origins bear no resemblance to the sequence reported here.

PMID:
1575516
DOI:
10.1016/0003-9861(92)90480-k
[Indexed for MEDLINE]

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