Title

Purification Of Acetyllactosamine-Specific Tomato Lectin By Erythroglycan-Sepharose Affinity Chromatography

Document Type

Article

Publication Date

1-1-1989

Abstract

Tomato lectin is specific for oligomers of poly-N-acetyllactosamine containing 3 repeating Gal(£l-4) GlcNAc (£ 1–3) (01-3)-disaccharides. As such it is highly useful for purifying oligosaccharides or glycopeptides with poly-N-acetyllactosamine character. We have found the lectin very useful as an affinity reagent for-isolating glycoproteins or glycoprotein domains having poly-N-acetyllactosamine glycosylation. Conventional preparation of tomato lectip by ovomucoid-Sepharose affinity chromatography was found to be unsatisfactory due to instability of column and bleeding of ovomucoid into eluents requiring the necessity for additional purification steps following affinity chromatography. We prepared a column of human erythrocyte band 3 carbohydrate glycopeptide (erythroglycan) attached to Sepharose as an affinity matrix. The purification of tomato lectin to homogeneity in one step on this column matrix is described in this report. © 1989, Taylor & Francis Group, LLC. All rights reserved.

Publication Source (Journal or Book title)

Preparative Biochemistry

First Page

341

Last Page

350

This document is currently not available here.

Share

COinS