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Article (Scientific journals)
Isolation and characterization of the C3b-binding entity of C3b-receptor from human erythrocytes.
Mussel, H. H.; Ehlen, T.; Schmitt, Michèle et al.
1982In Immunology letters, 4 (1), p. 1-6
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Keywords :
Animals; Antigens/immunology; Chemical Phenomena; Chemistry; Complement C3b/immunology/isolation & purification; Complement C3b Inactivator Proteins/pharmacology; Erythrocytes/analysis/immunology; Guinea Pigs; Humans; Immune Adherence Reaction; Monosaccharides/pharmacology; Rabbits; Receptors, Complement/isolation & purification; Rosette Formation
Abstract :
[en] Applying 2 M KBr, membranes of Ehu were solubilized. By C3-affinity chromatography an activity could be isolated that inhibited the immune adherence reaction and C3b-dependent rosette formation. Since this material did not agglutinate EAC14oxy23b we termed it monovalent C3b receptor (mC3bR). PAGE and SDS-PAGE and staining with Coomassie brilliant blue and PAS reagent revealed a single glycoprotein band with a mol. wt. of 55,000-60,000 daltons and an electrophoretic mobility comparable to ovalbumin. This mC3bR proved to be antigenetically related to gp 205 [17]. The potential of mC3bR to react with C3b-carrying particles was not destroyed by heat and trypsin treatment but by neuraminidase or periodic acid treatment suggesting that mC3bR reacted by its carbohydrate moiety with C3b. As by mC3bR, immune adherence could be inhibited by D-glucose and D-galactose but not by their optical antipodes, L-glucose and L-galactose.
Disciplines :
Cardiovascular & respiratory systems
Author, co-author :
Mussel, H. H.
Ehlen, T.
Schmitt, Michèle ;  University of Luxembourg > Central Administration > Student Department
Kazatchkine, M. D.
Neyses, Ludwig ;  University of Luxembourg > Research Office
Dierich, M. P.
Language :
English
Title :
Isolation and characterization of the C3b-binding entity of C3b-receptor from human erythrocytes.
Publication date :
1982
Journal title :
Immunology letters
ISSN :
0165-2478
Volume :
4
Issue :
1
Pages :
1-6
Peer reviewed :
Peer reviewed
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