Incorporation of amino acid analogs interferes with the processing of the asparagine-linked oligosaccharide of the MOPC-46B kappa light chain.

The incorporation of the leucine analog, beta-hydroxyleucine, or the isoleucine analog, 4-thiaisoleucine, into the MPOC-46B kappa chain interfered with the processing of the oligosaccharide moiety of newly synthesized light chains. Analog-containing chains were secreted with endo-beta-N-acetylglucosaminidase H-sensitive oligosaccharides instead of the normal complex, endo-beta-N-acetylglucosaminidase H-resistant oligosaccharide. The incorporation of the analogs did not significantly decrease the overall secretion of the MPOC-46B-related proteins. These data form the basis for the hypothesis that the presence of the analog in the protein alters the peptide configuration sufficiently to prevent the processing of precursor high mannose oligosaccharides to complex oligosaccharides.