Linked Life Data

6165395

Source:http://linkedlifedata.com/resource/pubmed/id/6165395

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1981-8-20
pubmed:abstractText
Clostridium perfringens type A enterotoxin was activated about 3-fold by treatment with trypsin, without an observed change in molecular weight. On denaturation in 8 M urea, the trypsinated enterotoxin lost a small peptide of about 4000 daltons. The single cysteine residue of enterotoxin was in the small peptide together with seven out of nine residues of proline. Trypsin activation, without removal of the small peptide, increased the 'outside' number of amino groups from eight to eleven. The trypsin treatment of the enterotoxin did not change the antigenic properties of the protein. Glycine was the C-terminal residue of the native enterotoxin while the dansyl alpha-amino acid of the N-terminal could not be identified.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
29
pubmed:volume
668
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
325-32
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1981
pubmed:articleTitle
Trypsin activation of enterotoxin from Clostridium perfringens type A: fragmentation and some physicochemical properties.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't