Structural relationships between the NADH dehydrogenases ofParacoccus denitrificansand bovine heart mitochondria as revealed by immunological cross-reactivities
| Autor: | Michael W. J. Cleeter, Christina L. George, C. lan Ragan, Stuart J. Ferguson |
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| Rok vydání: | 1986 |
| Předmět: |
Protein subunit
Biophysics Respiratory chain Cross Reactions Mitochondrion Biochemistry Mitochondria Heart Structural Biology Genetics Immmoblotting Animals Molecular Biology Cytochrome Reductases Paracoccus denitrificans chemistry.chemical_classification biology NADH dehydrogenase NADH Dehydrogenase Cell Biology biology.organism_classification Molecular biology Mitochondria Molecular Weight Enzyme chemistry Cytoplasm (Paracoccus denitrificans) biology.protein Cattle Antibody |
| Zdroj: | FEBS Letters. 198:135-139 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/0014-5793(86)81199-1 |
| Popis: | An antibody raised against two subunits (Mr, 48000 and 25000) of NADH dehydrogenase from Paracoccusdenitrificans cross-reacts with one of more than 20 polypeptides that form the bovine heart mitochondrial NADH dehydrogenase. The cross-reacting subunit has Mr, 51000 and is believed to be the NADH-binding subunit of the enzyme. Antibodies raised against certain subunits of the bovine heart NADH dehydrogenase were tested for cross-reactivity withP. denitrificans cytoplasmic membranes. Of those tested, only one, an antibody specific for the 49 kDa subunit of mitochondrial NADH dehydrogenase, cross-reacted with the bacterial membranes. It recognised a polypeptide of approximate Mr, 46000. This is an indication for a previously undetected third subunit of NADH dehydrogenase from P. denitrificans. The immunological crossreactions indicate that the NADH dehydrogenases from P. denitrificans and bovine heart mitochondria are related structurally. |
| Databáze: | OpenAIRE |
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