rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
1-2
|
pubmed:dateCreated |
1989-9-21
|
pubmed:abstractText |
Botulinum neurotoxin type D and exoenzyme C3 have been separately purified from Clostridium botulinum strain D-1873 to apparent homogeneity. Both ADP-ribosylated a rat liver cytosolic protein of 24 kDa. The N-terminal amino acid sequence of C3 was determined and showed a low degree of homology with those of the light and heavy chains of neurotoxins of various types which have been reported previously. However, a polyclonal antibody raised against C3 cross-reacted with the light chains, but not with the heavy chains, of type C1 and D neurotoxins. Furthermore, a monoclonal antibody recognizing the light chains of type C1 and D neurotoxins interacted with C3. These results suggest that the light chain of type C1 or D neurotoxin and exoenzyme C3 share at least one epitope in common with each other.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Jul
|
pubmed:issn |
0014-5793
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
31
|
pubmed:volume |
252
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
83-7
|
pubmed:dateRevised |
2010-11-18
|
pubmed:meshHeading |
pubmed-meshheading:2474453-ADP Ribose Transferases,
pubmed-meshheading:2474453-Adenosine Diphosphate Ribose,
pubmed-meshheading:2474453-Amino Acid Sequence,
pubmed-meshheading:2474453-Antibodies, Monoclonal,
pubmed-meshheading:2474453-Blotting, Western,
pubmed-meshheading:2474453-Botulinum Toxins,
pubmed-meshheading:2474453-Clostridium botulinum,
pubmed-meshheading:2474453-Cross Reactions,
pubmed-meshheading:2474453-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:2474453-Enzyme-Linked Immunosorbent Assay,
pubmed-meshheading:2474453-Epitopes,
pubmed-meshheading:2474453-Molecular Sequence Data
|
pubmed:year |
1989
|
pubmed:articleTitle |
Immuno-crossreactivity between botulinum neurotoxin type C1 or D and exoenzyme C3.
|
pubmed:affiliation |
Department of Biochemistry, Faculty of Pharmaceutical Sciences, Hokkaido University, Japan.
|
pubmed:publicationType |
Journal Article,
Comparative Study
|