Monoclonal antibodies recognizing the secreted and membrane domains of the IgA dimer receptor
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Conformational changes occurring upon membrane binding and subsequent insertion of staphylococcal alpha-toxin were studied using complementary spectroscopic techniques. Experimental conditions were established where binding could be uncoupled from membrane ...
Batch cultures of a mouse/mouse hybridoma cell line secreting a dimeric IgA were performed in combination with a membrane process for the continuous removal of ammonia from the culture medium. The latter involves hydrophobic porous membranes with an assocd ...
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A review with many refs. Ammonia has been reported to be toxic and inhibitory for mammalian cell cultures for many years. Redn. of growth rates and maximal cell densities in batch cultures, changes in metabolic rates, perturbation of protein processing and ...
The receptor responsible for the transepithelial transport of IgA dimer antibodies is a transmembrane glycoprotein known as membrane secretory component (SCm). During transport, the membrane anchoring domain is cleaved and the ectoplasmic domain of the rec ...
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Secretory component (SC), synthesized as a transmembrane protein, acts as the receptor that binds IgA dimers and mediates their transepithelial transport. Cleavage of the receptor (membrane SC) apparently occurs during transport and a fragment, the secrete ...
