Open AccessInteraction of Concanavalin A with Native and Denatured Forms of Jackbean α‐ d ‐Mannosidase
Author(s) -
BOWLES Dianna J.,
CHAPLIN Martin F.,
MARCUS Susan E.
Publication year - 1983
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1983.tb07193.x
Subject(s) - oligosaccharide , mannosidase , concanavalin a , chemistry , swainsonine , glycoprotein , protein subunit , denaturation (fissile materials) , enzyme , hydrolysis , biochemistry , in vitro , nuclear chemistry , gene
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.