Isolation and characterization of the C3b-binding entity of C3b-receptor from human erythrocytes |
| |
| Authors: | H.-H. Mussel T. Ehlen M. Schmitt M.D. Kazatchkine L. Neyses M.P. Dierich |
| |
| Affiliation: | 1. Institute for Medical Microbiology, Johannes Gutenberg University, Hochhaus Augustusplatz, D-6500 Mainz, F.R.G.;1. Clinique Medicale, Hôpital Broussais, Paris, France |
| |
| Abstract: | 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 EAC14oxy 23b we termed it monovalent C3b receptor (mC3bR). PAGE and SDS-PAGE and staining with Coomassie brillant 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. |
| |
| Keywords: | EDTA ethylenediaminetetraacetic acid PMSF phenylmethylsulfonylfluoride human erythrocytes PBS phosphate-buffered saline SDS sodium dodecylsulfate mC3bR monovalent C3b-receptor I C3b inactivator sheep erythrocyte coated with antibody, C1, C4, oxidized C2, and C3 H factor H of the alternative pathway (earlier termed β1H) complement receptor-positive cells gp 205 glycoprotein with an apparent mol. wt. of 205,000 daltons [16] (? C3b-receptor, see ref. 17) SDS-PAGE sodium dodecylsulfate polyacrylamide gel-electrophoresis PAS periodic acid schiff VBS veronal-buffered saline VBS-S veronal-buffered saline-containing sucrose |
| 本文献已被 ScienceDirect 等数据库收录！ |
|
