• KSBB Journal
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• v.24 no.5
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• pp.458-462
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• 2009

Silk fibroin is a structural protein from Bombyx mori and can be sulfated to provide biofunctional polypeptides showing antiviral and anticoagulating activities. However, the sulfated fibroins have not been characterized enough to present their compositions and structures. In this report, sulfation reaction was investigated by varying the reaction temperature and sulfuric acid concentration and analysis of the resulting peptides were carried out. The degree of sulfation was proportion to sulfuric acid concentration but the maximum product yield was obtained at $60^{\circ}C$ and 5% of sulfuric acid concentration. FT-IR spectrum, UV absorption and NMR spectrum support that o-sulfate ester was formed at the hydroxyl group of serine and tyrosine residues. Size exclusion chromatography identified that sulfated fibroin was composed of a highly hydrolyzed polypeptide mixtures and peptides of relatively higher molecular weight.