Biotinylation of protein complexes may lead to aggregation as well as to loss of subunits as revealed by Blue Native PAGE

Journal of Immunological Methods

Volumn 252, Issue 1-2, 2001, Pages 171-174

  Schamel, Wolfgang W A ^a,b  

^a MAX PLANCK INSTITUTE OF IMMUNOBIOLOGY AND EPIGENETICS   (Germany)

^b UNIVERSIDAD AUTÓNOMA DE MADRID   (Spain)

Author keywords

BCR; Biotin; Blue Native; Protein complex; Stoichiometry; Structure

Indexed keywords

B LYMPHOCYTE RECEPTOR;

ARTICLE; BIOTINYLATION; CELL SURFACE; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ANALYSIS; PROTEIN STRUCTURE; STOICHIOMETRY;

EID: 0035371858     PISSN: 00221759     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-1759(01)00357-X     Document Type: Article

References (9)

1. The Tim core complex defines the number of mitochondrial translocation contact sites and can hold arrested preproteins in the absence of matrix Hsp70-Tim44
2. Two new proteins preferentially associated with membrane-immunoglobulin D
3. Immunochemical detection of proteins biotinylated on nitrocellulose replicas
4. The TIM17.23 preprotein translocase of mitochondria: Composition and function in protein transport into the matrix
5. Antigen receptors on B lymphocytes
6. Analysis of molecular masses and oligomeric states of protein complexes by blue native electrophoresis and isolation of membrane protein complexes by two-dimensional native electrophoresis
7. Detection of proteins after biotinylation within polyacrylamide gels (BIG method)
8. Monomeric and oligomeric complexes of the B cell antigen receptor