Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1994-1-31
pubmed:abstractText
In this study, we tried to purify the antibacterial fragments of guinea-pig major basic protein (MBP) using Staphylococcus aureus. The antibacterial activity of MBP was not affected by the pyridylethylation, suggesting that the disulfide bonds were not necessary for the antibacterial activity. When pyridylethylated-MBP was digested with alpha-chymotrypsin, the four potent antibacterial fragments (fragment V (Arg105-Tyr119), fragment IX (Thr1-Phe67), fragment X (Ile54-Leu97) and fragment XIII (Arg25-Phe67)) were isolated by reverse-phase high-performance liquid chromatography. Anti-MBP monoclonal antibody, BMK-13 neutralized the antibacterial activity of PE-MBP and fragments IX, X and XIII, but not the activity of fragment V, suggesting that Ile54-Phe67, the common amino-acid sequence of fragments IX, X and XIII, might be involved in the antibacterial activity of MBP. In fact, the synthetic peptide, Ile54-Phe67 exerted the antibacterial activity, and the activity was neutralized with BMK-13. The antibacterial activity of Ile54-Phe67 was lost by the modification with peptidylarginine deiminase which converted arginine residue to citrulline residue, suggesting that the arginine residues may be important for the antibacterial activity.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
8
pubmed:volume
1203
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
236-42
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Purification of the antibacterial fragments of guinea-pig major basic protein.
pubmed:affiliation
Department of Biochemistry, School of Medicine, Juntendo University, Tokyo, Japan.
pubmed:publicationType
Journal Article