Interaction of Concanavalin A with Native and Denatured Forms of Jackbean α‐d‐Mannosidase

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Abstract

Tetrameric α‐d‐mannosidase from jackbean is a glycoprotein containing at least one mannosylated oligosaccharide. In the native enzyme, the oliosaccharide is sterically masked from interaction with either endoglucosaminidase H or concanavalin A. Denaturation into subunits permits endoglucosaminidase hydrolysis and removal of the oligosaccharide. The mannosyl residues are attached only to the heavy type of subunit. Removal of the oligosaccharide(s) from the denatured heavy subunit requires the joint action of both α‐d‐mannosidase and N‐acetyl‐β‐d‐glucosaminidase. Copyright © 1983, Wiley Blackwell. All rights reserved

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BOWLES, D. J., CHAPLIN, M. F., & MARCUS, S. E. (1983). Interaction of Concanavalin A with Native and Denatured Forms of Jackbean α‐d‐Mannosidase. European Journal of Biochemistry, 130(3), 613–618. https://doi.org/10.1111/j.1432-1033.1983.tb07193.x

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