Antibody-mediated activation of a defective beta-D-galactosidase: dimeric form of the activatable mutant enzyme.
AUTOR(ES)
de Macario, E C
RESUMO
Sedimentation analyses of AMEF, an activatable mutant beta-D-galactosidase (beta-D-galactoside galactohydrolase, EC 3.2.1.23), and the products of its reaction with Fab fragments of activating antibody show that this enzyme exists mainly as 10S dimers. Activation of AMEF by purified antibody resulted in formation of 16S tetramers. A unifying hypothesis postulating a dimer--tetramer equilibrium accounts for this observation as the counterpart of inactivation, which was shown to involve the breakdown of tetramers into inactive subunits [Roth, R. A. & Rotman, B. (1975) Biochem. Biophys. Res. Commun. 67, 1382--1390]. Conditions are described under which AMEF loses the specific antigenic determinant(s) responsible for binding activating antibody, allowing its subsequent use as an absorption to obtain immunologically purified activating antibody,
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=411328Documentos Relacionados
- Antibody-mediated activation of a defective beta-D-galactosidase extracted from an Escherichia coli mutant.
- Antibody-mediated activation of genetically defective Escherichia coli beta-galactosidases by monoclonal antibodies produced by somatic cell hybrids.
- Antibody-mediated cytotoxicity in rheumatoid arthritis.
- New Concepts in Antibody-Mediated Immunity
- Diversity of Antibody-Mediated Immunity at the Mucosal Barrier