Abstract
The sialoglycopeptide (PSGP-A), isolated from the degelled skin of the fish Mastacembalus armatus, contained sialic acids (NANA and NGNA, 13.5%), GlcNAc (19.3%), Gal (14.7%), Man (12.6%), Fux (2.5%), and amino acids of which Asp, Ser, Thr, and Pro preponderated. Affinity chromatography showed that the two sialic acids were integral parts of the same glycopeptide molecules. The carbohydrate portion was linked through GlcNAc to Asn of the peptide core. Methylation analysis of PSGP-A and its degradation products and periodate-oxidation studies indicated a structure for the carbohydrate portion of PSGP-A which resembled those of other sialoglycopeptides having similar carbohydrate compositions.
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