title: Purification and characterization of anticomplement factor (cobra venom factor) from the Naja naja atra venom.
abstract: Anticomplement factor (cobra venom factor) from the venom of Naja naja atra was purified by means of successive chromatography on DEAE-cellulose, Sephadex G-200 and Sepharose CL-6B. The purified anticomplement factor was homogeneous as judged by polyacrylamide discontinuous gel electrophoresis at pH 9.4. The yield from 3.0 g of the crude venom was approx. 28 mg. The molecular weight was estimated to be about 156 000 by SDS-polyacrylamide gel electrophoresis. The isoelectric point was about 5.2. SDS-polyacrylamide gel electrophoresis of the anticomplement factor in the presence of dithiothreitol demonstrated that the molecule possesses three different polypeptide chains cross-linked covalently to one another by disulfide bridge(s). By SDS-polyacrylamide gel electrophoresis, the molecular weight of each subunit was determined to be approx. 77000, 47500 and 29 000, respectively. All subunits were stained with Coomassie brilliant blue G-250 and periodate-Schiff reagent, indicating these subunits to be glycoprotein. Distribution of the anticomplement factor in various snake venoms, which shows cross-reactivity against the anti-Naja naja atra anticomplement factor antiserum, was examined. From the results, all venoms belonging to cobra family in the Elapidae tested so far were found to contain such cross-reactivity.
mesh_terms: D000596:Amino Acids / Q000032:analysis; D004546:Elapid Venoms / Q000032:analysis* / Q000276:immunology / Q000302:isolation & purification*; D000939:Epitopes; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D005779:Immunodiffusion; D007526:Isoelectric Point; D008970:Molecular Weight
chemical_list: D000596:Amino Acids; D004546:Elapid Venoms; D000939:Epitopes; C016310:cobra venom factor