Linked Life Data

1630298

Source:http://linkedlifedata.com/resource/pubmed/id/1630298

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1992-8-20
pubmed:abstractText
The amino acid sequences of eight variants of thermostable direct hemolysin (TDH) and a TDH-related hemolysin, deduced from nucleotide sequences, were compared. Fourteen amino acid residues, mainly within conserved regions, were chosen to prepare mutant TDHs with one or two amino-acid replacements by site-directed mutagenesis. Of the 25 mutant TDHs prepared, those with replacements of Trp65 (Trp65-His65, Trp65-Tyr65, Trp65-Leu65) or Leu66 (Leu66-Ser66) showed very significant reduction (more than 150-fold) of hemolytic activity. Several other mutant TDHs with replacements at Lys45, Arg46 and Gly90 showed weaker hemolytic activity than the wild-type TDH, but extents of reduction in hemolytic activity were much less than for mutant TDHs with replacements at Trp65 and Leu66. These results indicate that Trp65 and Leu66 are very important for the hemolytic activity of TDH.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0882-4010
pubmed:author
pubmed:issnType
Print
pubmed:volume
12
pubmed:geneSymbol
tdh, trh
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
279-87
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
Examination by site-directed mutagenesis of the amino acid residues of the thermostable direct hemolysin of Vibrio parahaemolyticus required for its hemolytic activity.
pubmed:affiliation
Department of Microbiology, Faculty of Medicine, Kyoto University, Japan.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't