Effects of iodipamide on human C3 and factor B in vitro |
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Authors: | Paul J. Durda Robert J. Pagano Norman Bauman John A. Brockman |
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Affiliation: | From the Biological Research Department, Metabolic Disease Research Section, Medical Research Division, American Cyanamid Co., Lederle Laboratories, Pearl River, N. Y., USA |
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Abstract: | The effects of iodipamide on C3 and factor B in normal human serum and in purified form have been examined by immunoelectrophoresis and sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). Temperature-dependent changes in immunoelectrophoretic profile's have been observed; however, these are not the same as those obtained after treatment of normal human serum (NHS) with cobra venom factor Naja naja. Analyses of iodipamide-treated NHS and purified C3 and factor B by reducing SDS-PAGE indicate that no macromolecular changes have occurred in C3 and factor B that can be ascribed to proteolysis (i.e., activation). The changes observed in C3 and factor B, including loss of hemolytic activity, appear to be due to direct interactions between iodipamide and C3 and factor B. In the case of factor B, iodipamide treatment at 37° C induces aggregation, which is reversible upon reduction with β-mercaptoethanol. |
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Keywords: | RCM Radiographic contrast media CVF Cobra venom factor HSA Human serum albumin BSA Bovine serum albumin GVB Gelatin Veronal-buffered saline GVB containing calcium magnesium Half-strength GVB rendered isotonic by addition of D-glucose containing calcium magnesium gelatin PBS Phosphate-buffered saline IEP Immunoelectrophoresis SDS-PAGE Sodium dodecyl sulfate polyacrylamide gel electrophoresis β-ME β-Mercaptoethanol NHS Normal human serum EAC43 Sheep erythrocytes sensitized with anti-sheep red blood cell antibody complement components of C4 C3 Ba Bb Proteolytic cleavage fragments of factor B Bi Hemolytically inactive Total hemolytic complement activity |
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