Chemical Modification of Tryptophan Residues in Castor Bean Hemagglutinin

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概要

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• Modification of tryptophan residues in castor bean hemagglutinin (CBH) with N-bromosuccinimide (NBS) was investigated in detail. Tryptophan residues accessible to NBS increased with lowering pH and six tryptophan residues/mol were oxidized at pH 3.0, while two tryptophan residues/mol were oxidized at pH 5.0. From the pH-dependence curve for tryptophan oxidation, we suggest that -the extent of modification of tryptophan in CBH is influenced by an ionizable group with pKa=3.6. The saccharide-binding activity was decreased greatly by modification of tryptophan concomitantly with a loss of fluorescence. A loss of the saccharide-binding activity was found to be principally due to the modification of two tryptophan residues/mol located on the surface of the protein molecule. In the presence of raffinose, two tryptophan residues/mol remained unmodified with retention of fairly high saccharide-binding activity. The results suggest that one tryptophan residue is involved in each saccharide-binding site on each B-chain of CBH.

• 社団法人 日本農芸化学会の論文

著者

• FUNATSU Gunki

  Laboratory of Biochemistry, Faculty of Agriculture, Kyushu University

• Absar Nural

  Laboratory Of Biochemistry Faculty Of Agriculture Kyushu University

• Funatsu Gunki

  Laboratory Of Biochemistry And ** Laboratory Of Protein Chemistry & Engineering Faculty Of Agric

• Yamasaki Nobuyuki

  Laboratory Of Agricultural Process Engineering Faculty Of Agriculture Kyushu University

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