SEARCH:   Advanced

Blood, Vol. 111, Issue 2, 624-632, January 15, 2008 This Article Abstract Full Text Services Email this article to a friend Alert me to new issues of the journal Rights and Permissions Citing Articles Citing Articles via CrossRef Membrane cofactor protein mutations in atypical hemolytic uremic syndrome (aHUS), fatal Stx-HUS, C3 glomerulonephritis, and the HELLP syndrome Blood Fang et al. 111: 624 Supplemental materials for: Fang et al Files in this Data Supplement: Figure S1. Analysis of MCP binding to C3b (A) and C4b (B) (JPG, 57.9 KB) - Binding assays were performed at 25 mM salt concentration. CHO cell lysates (5 × 106 to 25 × 106 MCP molecules as measured by ELISA) of R69W, A304V, and wild type from both transient transfections and stable cell lines were used. Data represent the mean ± SD for 10 experiments. Figure S2. Analysis of C3b binding employing purified proteins (JPG, 57.4 KB) - Binding assay was performed at 25 mM NaCl. Diluted CHO cell lysate extracts (5 × 106 to 25 × 106 MCP molecules as quantitated in ELISA) of R69W, A304V, and wild type were purified by using TRA-2-10-Sepharose beads. Mutant and wild-type MCP were eluted with 50 mM ethylamine, pH 11.5 and then neutralized with 250 mM of sodium acetate buffer (pH 4.6). Figure S3. The AP does not spontaneously activate on unsensitized CHO cells (JPG, 61.8 KB) - There is no C3d fragment deposited in the absence of a sensitizing antibody with 10% C7d serum for 60 min in Mg2+-EGTA. Representative experiment of four. Same result is obtaind with 4 or 8.3 mg/ml of sensitizing Ab or with 30% serum. This Article Abstract Full Text Services Email this article to a friend Alert me to new issues of the journal Rights and Permissions Citing Articles Citing Articles via CrossRef

	Copyright © 2009 by American Society of Hematology         Online ISSN: 1528-0020