Correlation between carbohydrate‐binding specificity and amino acid sequence of carbohydrate‐binding regions of Cytisus‐type anti‐H(O) lectins

Open Access
Publisher Website
Google Scholar
Abstract
A carbohydrate‐binding peptide of the di‐N‐acetylchitoblose‐binding Cytisus sessilifolius anti‐H(O) lectin I (CSA‐I) was isolated from the endoproteinase Asp‐N digest of CSA‐I by affinity chromatography on a column of N‐acetyl‐d‐glucosamine oligomer‐Sepharose (GIcNAc oligomer‐Sepharose). The amino acid sequence of the carbohydrate‐binding peptide of CSA‐I was determined to be DTYFGKTYNPW using a gas‐phase protein sequencer. This sequence corresponds to the sequence from Asp‐129 to Trp‐139 based on the primary structure of CSA‐I, and shows a high degree of homology to those of the putative carbohydrate‐binding peptide of the Laburnum alpinum lectin I (LAA‐I) (DTYFGKAYNPW) and of the Ulex europaeus lectin II (UEA‐II) (DSYFGKTYNPW). The binding of these three anti‐H(O) lectins is known to be inhibited by di‐N‐acetylchitobiose but not by l‐fucose. These results strongly suggest that there is a good correlation between the carbohydrate‐binding specificity and the amino acid sequence of the carbohydrate‐binding regions of di‐N‐acetylchitobiose‐binding lectins.

This publication has 25 references indexed in Scilit: