1986Agricultural and Biological ChemistryOpen access

Identification of the tryptophan residue located at the saccharide binding site of castor bean hemagglutinin.

Nurul Absar, Nobuyuki Yamasaki, Gunki Funatsu

Open full text 1 citations

Abstract

The tryptophan residue present at the saccharide-binding site of castor bean hemagglutinin (CBH) was identified.A peptide containing a modified tryptophan residue was isolated from the tryptic digest of S-carboxymethylated B-chain obtained from an inactive derivative of CBH(2-Oxa-CBH), in which two tryptophan residues/mol were oxidized with Af-bromosuccinimide, by gel filtration on a Sephadex G-50 followed by high performance liquid chromatography.Analytical data for the isolated peptide indicated that the tryptophan residue at position 131 on the B-chain was modified in 2-Oxa-CBH.From these and earlier results, it is suggested that the tryptophan residue at 131 on each Bchain is closely associated with the saccharide-binding activity of CBH.The specific role of tryptophan residue at 131 in the saccharide-binding site of CBHis also discussed.

Open-access reader

About this research paper

What this paper is about

The tryptophan residue present at the saccharide-binding site of castor bean hemagglutinin (CBH) was identified.A peptide containing a modified tryptophan residue was isolated from the tryptic digest of S-carboxymethylated B-chain obtained from an inactive derivative of CBH(2-Oxa-CBH), in which two tryptophan residues/mol were oxidized with Af-bromosuccinimide, by gel filtration on a Sephadex G-50 followed by high performance liquid chromatography.Analytical data for the isolated peptide indicated that the tryptophan residue at position 131 on the B-chain was modified in 2-Oxa-CBH.From these and earlier results, it is suggested that the tryptophan residue at 131 on each Bchain is closely associated with the saccharide-binding activity of CBH.The specific role of tryptophan residue at 131 in the saccharide-binding site of CBHis also discussed.

Why it matters

OpenAlex reports 1 citations for this work. Citation counts describe recorded attention and do not establish research quality.

Key contribution

A contribution statement is not available in the OpenAlex record.

Method / approach

Method details are not available in the OpenAlex metadata.

Main findings

Findings are not separately available in the OpenAlex metadata.

Limitations

Limitations are not available in the OpenAlex metadata.

Applications

Application details are not available in the OpenAlex metadata.

Available abstract

The tryptophan residue present at the saccharide-binding site of castor bean hemagglutinin (CBH) was identified.A peptide containing a modified tryptophan residue was isolated from the tryptic digest of S-carboxymethylated B-chain obtained from an inactive derivative of CBH(2-Oxa-CBH), in which two tryptophan residues/mol were oxidized with Af-bromosuccinimide, by gel filtration on a Sephadex G-50 followed by high performance liquid chromatography.Analytical data for the isolated peptide indicated that the tryptophan residue at position 131 on the B-chain was modified in 2-Oxa-CBH.From these and earlier results, it is suggested that the tryptophan residue at 131 on each Bchain is closely associated with the saccharide-binding activity of CBH.The specific role of tryptophan residue at 131 in the saccharide-binding site of CBHis also discussed.

Key concepts: Tryptophan, Residue (chemistry), Chemistry, Sephadex, Peptide, Size-exclusion chromatography, Binding site, Biochemistry

Related papers

Back to paper searchBrowse research topicsOriginal source
Identification of the tryptophan residue located at the saccharide binding site of castor bean hemagglutinin. — Research Paper | ScholarLens