Cytochrome P-450: hexameric structure of the purified LM4 form

K. N. Myasoedova, V. L. Tsuprun

Research output: Contribution to journalArticlepeer-review

20 Scopus citations

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 languageEnglish (US)
Pages (from-to)251-254
Number of pages4
JournalFEBS Letters
Volume325
Issue number3
DOIs
StatePublished - Jul 5 1993

Keywords

  • Cytochrome P-450
  • Hexamer
  • Immobilized protein
  • Quaternary structure

Fingerprint

Dive into the research topics of 'Cytochrome P-450: hexameric structure of the purified LM4 form'. Together they form a unique fingerprint.

Cite this