EXPRESSION OF THE CARBOHYDRATE-RECOGNITION DOMAIN OF BOVINE CONGLUTININ AND DEMONSTRATION OF ITS BINDING TO IC3B AND YEAST MANNAN

Authors
Citation
Bl. Lim et U. Holmskov, EXPRESSION OF THE CARBOHYDRATE-RECOGNITION DOMAIN OF BOVINE CONGLUTININ AND DEMONSTRATION OF ITS BINDING TO IC3B AND YEAST MANNAN, Biochemical and biophysical research communications, 218(1), 1996, pp. 260-266
Citations number
25
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Biology,Biophysics
ISSN journal
0006-291X
Volume
218
Issue
1
Year of publication
1996
Pages
260 - 266
Database
ISI
SICI code
0006-291X(1996)218:1<260:EOTCDO>2.0.ZU;2-O
Abstract
Bovine conglutinin is a collagenous C-type lectin (collectin) that is found in bovine serum. A recombinant protein, composed of the neck-reg ion and the carbohydrate binding domain of bovine conglutinin, has bee n overexpressed in E. coli. The recombinant protein has been successfu lly renatured and showed the same sugar binding specificity as the nat ive protein and was able to bind to yeast mannan and complement-activa ted immune complexes. The binding was calcium-dependent and was inhibi ted by N-acetylglucosamine. The concentration of N-acetylglucosamine r equired for 50% inhibition of binding to mannan was 1.77 mM for recomb inant conglutinin and 0.71 mM for native conglutinin, respectively. Th e recombinant conglutinin should be useful in the assay and purificati on of circulating immune complexes and for therapeutic purposes involv ing the removal of immune complexes from patient's plasma. (C) 1996 Ac ademic Press, Inc.