Linked Life Data

8670244

Source:http://linkedlifedata.com/resource/pubmed/id/8670244

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1996-8-6
pubmed:abstractText
Aprotinin is a protein proteinase inhibitor of 58 amino acids, located in bovine mast cells which also possesses antibacterial activity. Digestion of aprotinin by clostripain yielded three antimicrobial oligopeptide fragments with the sequences RPDFCLEPPYTGPCK (residues 1-15), IIRYFYNAKAGLCQTFVYGGCR (residues 18-39) and AKRNNFKSAEDCMRTCGGA (residues 40-58). With the exception of residues 16 (alanyl) and 17 (arginyl) they cover the whole aprotinin structure. The three oligopeptides were synthesized and found to exert a broad spectrum of antimicrobial activities. Most potent was oligopeptide IIRYFYNAKAGLCQTFVYGGCR which at a concentration of 7 x 10(-9) M exhibited a high bactericidal activity against the eleven gram-positive and gram-negative bacterial strains tested. None of the purified oligopeptides showed any antiproteolytic activity. Our results suggest that aprotinin has multiple antimicrobial domains which are independent of the antiproteolytic function of the original molecule.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
222
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
559-65
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Identification and isolation of the bactericidal domains in the proteinase inhibitor aprotinin.
pubmed:affiliation
Institute of Veterinary Physiology, University of Zürich, Switzerland.
pubmed:publicationType
Journal Article