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Cytochrome P‐450: hexameric structure of the purified LM4 form
Author(s) -
Myasoedova K.N.,
Tsuprun V.L.
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)81083-c
Subject(s) - random hexamer , chemistry , oligomer , protein quaternary structure , dispersity , cytochrome , glycerol , crystallography , polymer chemistry , biochemistry , enzyme , gene , protein subunit
Purified cytochrome P‐450 LM4 was found to be monodisperse in 20% glycerol by analytical ultracentrifugation. Its S 20,w value was quite similar to that of hexameric P‐450 LM2 . At lower glycerol concentrations the P‐450 LM4 oligomers showed a tendency to aggregate. The P‐450 LM4 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‐450 LM4 is a hexamer. This was confirmed by electron microscopy. The quaternary structure of the P‐450 LM4 was similar to that demonstrated earlier for P‐450 LM2 .