Abstract
Purified cytochrome P-450LM4 was found to be monodisperse in 20% glycerol by analytical ultracentrifugation. Its S20,w value was quite similar to that of hexameric P-450LM2. At lower glycerol concentrations the P-450LM4 oligomers showed a tendency to aggregate. The P-450LM4 oligomers were immobilized on Ultrogel A4 under conditions allowing only one covalent link to the matrix per oligomer. In the presence of SDS, the oligomers dissociated leaving only 1 6th of the initial amount of bound protein on the matrix, suggesting that the purified P-450LM4 is a hexamer. This was confirmed by electron microscopy. The quaternary structure of the P-450LM4 was similar to that demonstrated earlier for P-450LM2.
Original language | English (US) |
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Pages (from-to) | 251-254 |
Number of pages | 4 |
Journal | FEBS Letters |
Volume | 325 |
Issue number | 3 |
DOIs | |
State | Published - Jul 5 1993 |
Keywords
- Cytochrome P-450
- Hexamer
- Immobilized protein
- Quaternary structure