Isolation and fractionation of glycopeptides from porcine thyroglobulin.

摘要: 1. Glycopeptides were isolated by gel filtration on Sephadex G-25 and G-50 from a Pronase digest of porcine thyroglobulin. 2. Isolated glycopeptides separated into five main fractions column DEAE-Sephadex A-25. Of these I to III further purified SE-Sephadex C-25 or A-25 chromatography. Several the homogeneous paper electrophoresis. 3. Based chemical composition molecular weight fractionated glycopeptides, two distinct types heterosaccharide chain demonstrated. 4. One type unit consisted four eight residues mannose glucosamine had 1000–1700. The other contained sialic acid, fucose galactose in addition about 3600. 5. Mild alkaline treatment glycopeptide did not result destruction threonine serine. 2-Acetamido-1-N-(4-l-aspartyl)-2-deoxy-β-d-glucopyranosylamine was partial acid hydrolysates.