Abstract
Binding and functional properties of concanavalin A and its derivatives. I. Monovalent, divalent, and tetravalent derivatives stable at physiological pH.
Highlights
Ain the presence of the bifunctional reagent, hexamethylene diisocyanate, resulted in the covalent coupling of subunits from the two chemically distinct species
On the basis of a knowledge of the covalent and three-dimensional structure of Con A, we have previously examined a number of chemical derivatives of the lectin
Three key chemical reactions were applied to the Con A molecule: (a) photoaffinity labeling with a-N:,PhMan for inactivation of the saccharide-binding site [6, 8]; (b) treatment with succinic anhydride for dissociation of the native tetrameric molecule into dimers [7]; and (c) mixing of native Con A and succinyl-Con A leading to the formation of hybrid molecules consisting of one protomer of Con A and one protomer of succinyl-Con A [10]
Summary
All chemicals employed in this work were reagent grade and, unless otherwise specified, were used without further purification. The tubing was pretreated by heating at 60°C in 2% sodium carbonate solution, rinsing and heating in distilled water and in 1 rnM EDTA. It was stored at 4°C in 1 rnM EDTA orior to use. Con A was isolated from-jack bean meal (SchwarziMann) as described previously [14]. The purified Con A was treated with succinic anhvdride ihlatheson. Cbleman and Bell) and acetic anhvdride (Eastman Organic Chemicals,) to form succinyl-Con A and acetyl-Con A, respectively [7]. Fluorescein-labeled rabbit antibodies directed against mouse immunoglobulin were prepared as described previously [7]
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