Effect of reduction and alkylation on structure and function of rabbit IgG antibody—I. Effect on ability to activate complement depends on conditions of reduction |
| |
| Authors: | Betty Anne Johnson Louis G. Hoffmann |
| |
| Affiliation: | Department of Microbiology, College of Medicine, University of Iowa, Iowa City, IA 52242 U.S.A. |
| |
| Abstract: | Anaerobic reduction of rabbit IgG antibody with either dithiothreitol at pH 8.0 or 2-mercaptoethanol at pH 5.0 results in the production of antibody molecules which lack haemolytic activity yet whose interchain disulfide bonds remain intact. Aerobic reduction with 2-mercaptoethanol results in more haemolytic activity than can be accounted for by the residual amount of Ab with intact interchain bonds. Taken together, these findings suggest that the interheavy chain disulfide bond in rabbit IgG is not essential for interaction with complement but that an intraheavy chain bond is critical. |
| |
| Keywords: | 2ME 2-mercaptoethanol 2MEA 2 mercaptoethylamine DTT dithiothreitol DTE dithioerythritol PAGE polyacrylamide gel electrophoresis SDS sodium dodecyl sulfate DNP 2,4-dinitrophenyl BGG bovine gamma globulin TNP 2,4,6-trinitrophenyl BSA bovin serum albumin TBS PBS MOPS morpholinopropane sulfonic acid Tris trishydroxymethylaminomethane DATD,N N′-diallyltartardiamide TEMED, N, N, N′ N′-tetramethylethylenediamine Author to whom correspondence should be addressed. |
| 本文献已被 ScienceDirect 等数据库收录！ |
|
