Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1997-10-1
pubmed:abstractText
The bacteriocin produced by Lactococcus lactis ssp. lactis biovar. diacetylactis UL 719 was purified and characterized. Two peaks exhibiting antimicrobial activity were obtained after purification. Primary structure of the peptide of major peak 2 was identical to that of nisin Z when determined by Edman degradation and confirmed by DNA sequence analysis. The molecular mass as determined by mass spectrometry was 3346.39 +/- 0.40 Da for peak 1 and 3330.39 +/- 0.27 Da for peak 2, which suggests that peak 1 may correspond to an oxidized form of nisin Z. The two purified peaks exhibiting antimicrobial activity appear to correspond with oxidized and native forms of nisin Z.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
1364-5072
pubmed:author
pubmed:issnType
Print
pubmed:volume
83
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
133-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Note: genetic and biochemical characterization on nisin Z produced by Lactococcus lactis ssp. lactis biovar. diacetylactis UL 719.
pubmed:affiliation
Centre de recherche STELA, Université Laval, Queébec, Canada.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't