Linked Life Data

8319899

Source:http://linkedlifedata.com/resource/pubmed/id/8319899

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1993-8-5
pubmed:databankReference
pubmed:abstractText
The three components of the 'enterotoxin complex' have been purified and the sequence of the first 14-15 amino acids of the proteins determined. Limited homology was found in the N-terminal sequence of the three proteins. The molecular mass of the proteins was determined to be 48, 40 and 34 kDa, respectively. Only the 40-kDa protein was toxic to Vero cells, whilst the 34-kDa protein was found to be hemolytic. The sequence of the first 14 N-terminal amino acids of this protein was identical to the sequence of the sphingomyelinase residues 28-41 (the N-terminal after loss of the signal sequence), except for a change from Gln to Glu in position 33 of the sphingomyelinase sequence.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0378-1097
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
110
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
97-100
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Sphingomyelinase is part of the 'enterotoxin complex' produced by Bacillus cereus.
pubmed:affiliation
Department of Food Hygiene, Norwegian College of Veterinary Medicine, Oslo.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't