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Title: The receptor-binding domain of human alpha 2-macroglobulin. Isolation after limited proteolysis with a bacterial proteinase
Authors: Van Leuven, Freddy ×
Marynen, Peter
Sottrup-Jensen, L
Cassiman, Jean-Jacques
Van den Berghe, Herman #
Issue Date: Sep-1986
Series Title: Journal of Biological Chemistry vol:261 issue:24 pages:11369-73
Abstract: Limited proteolysis of human alpha 2-macroglobulin (alpha 2M) by a novel bacterial proteinase resulted in the isolation of a soluble 20-kDa domain. The isolated fragment contained the receptor recognition site, expressed on alpha 2M complexes, as it competed effectively with alpha 2M-trypsin for binding to the receptor on skin fibroblasts. The fragment also reacted with two monoclonal antibodies which define epitopes that are part of the receptor recognition site. Characterization of the 20-kDa domain showed it to contain an intact disulfide bridge, while its susceptibility to N-glycanase and reaction with concanavalin A indicated the presence of N-linked carbohydrate. The NH2-terminal sequence (Glu-Glu-Phe-Pro-Phe-Ala-Leu-Gly-Val-Glu-Thr-Leu-Pro-Glu-Thr-Cys-Asp-Glu -Pro) proved this fragment to constitute the COOH terminus of human alpha 2M. Proteolysis occurred at Lys1313-Glu which together with the observation that tosyllysine chloromethyl ketone was an effective inhibitor of the bacterial proteinase, would indicate the latter to hydrolyze preferentially peptide bonds carboxyl-terminal to lysine residues.
ISSN: 0021-9258
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Associated Laboratories - miscellaneous (-)
Molecular Genetics Section (-)
Human Mutations and Polymorphisms Section (-)
Clinical Genetics Section (-)
Forensic Biomedical Sciences
Department of Human Genetics - miscellaneous
× corresponding author
# (joint) last author

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