Immunochemical analysis of Micrococcus lysodeikticus (luteus) F1-ATPase and its subunits
| Autor: | Milton R.J. Salton, Carl Urban |
|---|---|
| Rok vydání: | 1983 |
| Předmět: |
Macromolecular Substances
ATPase Protein subunit Biophysics Antigen-Antibody Complex Immunoelectrophoresis Biology Biochemistry Micrococcus medicine chemistry.chemical_classification medicine.diagnostic_test Molecular mass Immune Sera Cell Biology Ouchterlony double immunodiffusion biology.organism_classification Molecular biology Molecular Weight Proton-Translocating ATPases Enzyme chemistry biology.protein Antibody Micrococcus luteus |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Bioenergetics. 724:230-240 |
| ISSN: | 0005-2728 |
| DOI: | 10.1016/0005-2728(83)90142-1 |
| Popis: | The F 1 -ATPase from Micrococcus lysodeikticus has been purified to 95% protein homogeneity in this laboratory and as all other bacterial F 1 s, possesses five distinct subunits with molecular weights ranging from 60 000 to 10 000 (Huberman, M. and Salton, M.R.J. (1979) Biochim. Biophys. Acta 547, 230–240). In this communication, we demonstrate the immunochemical reactivities of antibodies to native and SDS-dissociated subunits with the native and dissociated F 1 -ATPase and show that: (1) the antibodies generated to the native or SDS-dissociated subunits react with the native molecule; (2) all of the subunits comprising the F 1 are antigenically unique as determined by crossed immunoelectrophoresis and the Ouchterlony double-diffusion techniques; (3) antibodies to the SDS-denatured individual δ- and ϵ-subunits can be used to destabilize the interaction of these specific subunits with the rest of the native F 1 ; and (4) all subunit antibodies as well as anti-native F 1 were found to inhibit ATPase activity to varying degrees, the strongest inhibition being seen with antibodies to the total F 1 and anti-α- and anti-β-subunit antibodies. The interaction of specific subunit antibodies may provide a new and novel way to study further and characterize the catalytic portions of F 1 -ATPases and in general may offer an additional method for the examination of multimeric proteins. |
| Databáze: | OpenAIRE |
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