The zygomycete fungus (previously called ) secretes an aspartic proteinase containing two asparagine-linked, high-mannose type oligosaccharide chains at Asn and Asn. For structural elucidation of the carbohydrate moieties, the protein was divided into two portions, an N-terminal portion containing Asn and a C-terminal portion containing Asn, by a specific autocatalytic cleavage under alkaline conditions. Each of the asparagine-linked oligosaccharides was then released by peptide--glycosidase F digestion and pyridylaminated with a fluorescent reagent, 2-aminopyridine, at the reducing end. High-performance liquid chromatography analyses showed that the structure of the asparagine-linked oligosaccharide chain attached to residue Asn was Man GlcNAc, and that bound to residue Asn was Man GlcNAc and ManGlcNAc. These observations suggest that the processing of mannose residues in asparagine-linked oligosaccharides in the Golgi apparatus of resembles that in mammalian cells.


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