Immunochemical analysis of the subcommissural organ-Reissner’s fiber complex using antibodies against alkylated and deglycosylated glycoproteins of the bovine Reissner’s fiber

F.Nualart; E. M.Rodríguez

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Immunochemical analysis of the subcommissural organ-Reissner’s fiber complex using antibodies against alkylated and deglycosylated glycoproteins of the bovine Reissner’s fiber

机译：Immunochemical analysis of the subcommissural organ-Reissner’s fiber complex using antibodies against alkylated and deglycosylated glycoproteins of the bovine Reissner’s fiber

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Reissner’s fiber (RF) has been isolated, solubilized, and used to raise polycloncal 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 forLimax flavusagglutinin (affinity=∧sialic acid), whereas the 190-kDa compound (170 kDa after deglycosylation) keeps its affinity for this lectin suggesting that it hasN-linked andO-linked carbohydrate moieties, the three larger proteins probably having onlyN-linked carbohydra

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《cell and tissue research》 |1996年第1期|23-31|共页
作者
F.Nualart; E. M.Rodríguez;
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Instituto de Histología y Patología, Universidad Austral de Chile, Valdivia, Chile;

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Immunochemical analysis of the subcommissural organ-Reissner’s fiber complex using antibodies against alkylated and deglycosylated glycoproteins of the bovine Reissner’s fiber

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