Biotinylation of protein complexes may lead to aggregation as well as to loss of subunits as revealed by Blue Native PAGE
- 作者：Schamel ; Wolfgang W.A.
- 关键词：Blue Native ; Stoichiometry ; Biotin ; Structure ; BCR ; Protein complex ; BCR ; B cell antigen receptor ; BN-PAGE ; Blue Native polyacrylamide gel electrophoresis ; HC ; heavy chain ; Ig ; immunoglobulin ; LC ; light chain ; SDS-PAGE ; sodium dodecylsulfate polyacrylamid
- 刊名：Journal of Immunological Methods
- 出版年：2001
- 期刊代码：57_00221759
- 类别：imm
- 出版时间：June 1, 2001
- 卷：252
- 期：1-2
- 页码：171-174
- 文件大小：312 K
摘要
Blue Native polyacrylamide gel electrophoresis (BN-PAGE) is a high-resolution method for studying native protein complexes. Here, the migration behaviour of the B cell antigen receptor (BCR) in BN-PAGE with and without prior biotinylation of the cell surface, from which the complexes were purified, are compared. Non-biotinylated complexes appear as a single band, whereas biotinylated complexes display several bands, indicating that biotinylation leads to aggregation of complexes as well as to loss of subunits. Thus, BN-PAGE has limitations in studying multiprotein complexes. These results are used to gain insight into the stoichiometry of the complex.