Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
6
|
| pubmed:dateCreated |
1987-12-23
|
| pubmed:abstractText |
An immunoglobulin M (IgM) monoclonal antibody (mAb Elec-39), obtained against asymmetric acetylcholinesterase (AChE) from Electrophorus electric organs, also reacts with a fraction of globular AChE (amphiphilic G2 form) from Torpedo electric organs. This antibody does not react with asymmetric AChE from Torpedo electric organs or with the enzyme from other tissues of Electrophorus or Torpedo. The corresponding epitope is removed by endoglycosidase F, showing that it is a carbohydrate. The subsets of Torpedo G2 that react or do not react with Elec-39 (Elec-39+ and Elec-39-) differ in their electrophoretic mobility under nondenaturing conditions; the Elec-39+ component also binds the lectins from Pisum sativum and Lens culinaris. Whereas the Elec-39- component is present at the earliest developmental stages examined, an Elec-39+ component becomes distinguishable only around the 70-mm stage. Its proportion increases progressively, but later than the rapid accumulation of the total G2 form. In immunoblots, mAb Elec-39 recognizes a number of proteins other than AChE from various tissues of several species. The specificity of Elec-39 resembles that of a family of anti-carbohydrate antibodies that includes HNK-1, L2, NC-1, NSP-4, as well as IgMs that occur in human neuropathies. Although some human neuropathy IgMs that recognize the myelin-associated glycoprotein did not react with Elec-39+ AChE, mAbs HNK-1, NC-1, and NSP-4 showed the same selectivity as Elec-39 for Torpedo G2 AChE, but differed in the formation of immune complexes.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Acetylcholinesterase,
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Carbohydrates,
http://linkedlifedata.com/resource/pubmed/chemical/Epitopes,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoside Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin M,
http://linkedlifedata.com/resource/pubmed/chemical/Lectins,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Mannosyl-Glycoprotein...,
http://linkedlifedata.com/resource/pubmed/chemical/Plant Lectins,
http://linkedlifedata.com/resource/pubmed/chemical/lentil lectin,
http://linkedlifedata.com/resource/pubmed/chemical/pea lectin
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Dec
|
| pubmed:issn |
0022-3042
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
49
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
1720-31
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:2445915-Acetylcholinesterase,
pubmed-meshheading:2445915-Animals,
pubmed-meshheading:2445915-Antibodies, Monoclonal,
pubmed-meshheading:2445915-Antibody Specificity,
pubmed-meshheading:2445915-Carbohydrates,
pubmed-meshheading:2445915-Centrifugation, Density Gradient,
pubmed-meshheading:2445915-Electric Organ,
pubmed-meshheading:2445915-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:2445915-Electrophorus,
pubmed-meshheading:2445915-Epitopes,
pubmed-meshheading:2445915-Glycoside Hydrolases,
pubmed-meshheading:2445915-Immunoassay,
pubmed-meshheading:2445915-Immunoglobulin M,
pubmed-meshheading:2445915-Lectins,
pubmed-meshheading:2445915-Macromolecular Substances,
pubmed-meshheading:2445915-Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase,
pubmed-meshheading:2445915-Plant Lectins,
pubmed-meshheading:2445915-Species Specificity,
pubmed-meshheading:2445915-Tissue Distribution,
pubmed-meshheading:2445915-Torpedo
|
| pubmed:year |
1987
|
| pubmed:articleTitle |
An immunoglobulin M monoclonal antibody, recognizing a subset of acetylcholinesterase molecules from electric organs of Electrophorus and Torpedo, belongs to the HNK-1 anti-carbohydrate family.
|
| pubmed:affiliation |
Laboratoire de Neurobiologie, Ecole Normale Supérieure, Paris, France.
|
| pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
|