Title: Domain structure of human alpha 2-macroglobulin. Characterization of a receptor-binding domain obtained by digestion with papain
Authors: Sottrup-Jensen, L ×
Gliemann, J
Van Leuven, Freddy #
Issue Date: Oct-1986
Series Title: FEBS Letters vol:205 issue:1 pages:20-4
Abstract: Digestion of methylamine-treated alpha 2-macroglobulin (alpha 2M X MA) with catalytic amounts of papain at pH 4.5 has been investigated. Cleavage of Lys(1313)-Glu resulted in two major products, which could be separated by gel chromatography: a large disulfide bridged fragment set nearly the size of intact alpha 2M X MA, and an 18 kDa fragment, constituting the carboxy-terminal domain of alpha 2M. This domain contained the receptor recognition site, exposed as a result of cleavage of the internal beta-cysteinyl-gamma-glutamyl thiol esters in alpha 2M. Compared with alpha 2M-trypsin complex the apparent affinity for binding to rat hepatocyte receptors was 0.1 and 2% at 4 and 37 degrees C, respectively. The receptor-binding domain presumably forms a compact globular beta-barrel-type structure, stable at pH 2.5-9.0. Chemical modification experiments suggest that receptor binding is contributed by a determinant formed by the precise folding of the polypeptide chain.
ISSN: 0014-5793
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Associated Laboratories - miscellaneous (-)
Department of Human Genetics - miscellaneous
× corresponding author
# (joint) last author

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