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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
|
| pubmed:dateCreated |
1996-11-21
|
| pubmed:abstractText |
Reissner's fiber (RF) has been isolated, solubilized, and used to raise polyclonal antibodies. The present investigation has been designed: (1) to obtain antibodies against RF-glycoproteins in their native form (anti-RF-BI), after irreversible denaturation by alkylation (anti-RF-A), and after alkylation and deglycosylation by using endoglycosidase F (anti-RF-DE); (2) to use these antisera for a comparative immunocytochemical study of the subcommissural organ (SCO)-RF complex; (3) to establish the molecular mass of the deglycosylated RF-glycoproteins. Anti-RF-BI reacts with the SCO of all the species investigated. Anti-RF-A and anti-RF-DE only react with bovine SCO and RF. The three antisera stain the same bands in immunoblots of extracts of bovine SCO and RF, but anti-RF-A and anti-RF-DE reveal additional bands. The epitope common to all species reacting with anti-RF-BI is thus probably conformational in nature and associated with the integrity of the disulfide bonds. The lack of antibodies against conserved sequential epitopes in anti-RF-A does not support previous assumptions on the conserved nature of the SCO secretion. After deglycosylation by using endoglycosidase F, the RF-glycoproteins present a reduction in their molecular mass ranging between 10% and 25%. The three larger compounds (450, 300, and 230 kDa) lose their affinity for Limax flavus agglutinin (affinity = sialic acid), whereas the 190-kDa compound (170 kDa after deglycosylation) keeps its affinity for this lectin suggesting that it has N-linked and O-linked carbohydrate moieties, the three larger proteins probably having only N-linked carbohydrates.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Extracts,
http://linkedlifedata.com/resource/pubmed/chemical/Cerebrospinal Fluid Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Epitopes,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Oct
|
| pubmed:issn |
0302-766X
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
286
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
23-31
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:8781209-Alkylation,
pubmed-meshheading:8781209-Animals,
pubmed-meshheading:8781209-Antibodies, Monoclonal,
pubmed-meshheading:8781209-Antibody Specificity,
pubmed-meshheading:8781209-Brain Chemistry,
pubmed-meshheading:8781209-Cattle,
pubmed-meshheading:8781209-Cell Extracts,
pubmed-meshheading:8781209-Cerebrospinal Fluid Proteins,
pubmed-meshheading:8781209-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:8781209-Epitopes,
pubmed-meshheading:8781209-Glycoproteins,
pubmed-meshheading:8781209-Glycosylation,
pubmed-meshheading:8781209-Immunoblotting,
pubmed-meshheading:8781209-Immunohistochemistry,
pubmed-meshheading:8781209-Molecular Weight,
pubmed-meshheading:8781209-Nerve Fibers,
pubmed-meshheading:8781209-Spinal Cord,
pubmed-meshheading:8781209-Subcommissural Organ
|
| pubmed:year |
1996
|
| pubmed:articleTitle |
Immunochemical analysis of the subcommissural organ-Reissner's fiber complex using antibodies against alkylated and deglycosylated glycoproteins of the bovine Reissner's fiber.
|
| pubmed:affiliation |
Instituto de Histología y Patología, Universidad Austral de Chile, Valdivia, Chile.
|
| pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
|