Abstract
Kidney mitochondrial ferredoxin (renodoxin) is a component of the cytochrome P-450-dependent enzymatic system whose main function is the hydroxylation of vitamin D3 in the 1a- and 24-positions. The complete amino acid sequence of renodoxin was determined by protein chemistry and mass spectrometry. The mature renodoxin has 128 amino acid residues. The N- and C-terminal regions of renodoxin are subject to proteolytic modification, this being the origin of heterogeneous molecular mass (from 14,200 to 12,400 kD) of purified protein preparations. The antigenic structure of renodoxin was studied using antibodies to peptide fragments of a homologous protein, adrenodoxin.
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REFERENCES
Ponchon, C., and DeLuca, H. F. (1969) J. Clin. Invest., 48, 1273-1279.
Maruya, N., Hiwatashi, A., Ichikawa, Y., and Yamano, T. (1983) J. Biochem., 93, 1239-1247.
Driskoll, W. J., and Omdahl, J. L. (1986) J. Biol. Chem., 261, 4122-4125.
Lobanov, N. A., Vlasova, T. M., and Adamovich, T. B. (1990) Biokhimiya, 55, 1059-1064.
Laemmli, U. K. (1970) Nature, 227, 680-685.
Hayashi, R. (1977) Meth. Enzymol., 47, 84-93.
Lapko, V. N., Adamovich, T. B., Kirillova, N. M., Lapko, A. G., Budris, M. V., and Martinovich, L. G. (1986) Vestsi Akad. Navuk BSSR, 6, 67-72.
Gray, W. R., and Hartly, B. C. (1963) Biochemistry, 89, 235-238.
Walker, J. E., Fearnley, I. M., and Blows, R. A. (1986) Biochem. J., 237, 73-84.
Lapko, V. N., Smith, D. L., and Smith, J. B. (2000) J. Mass Spectrom., 35, 572-575.
Ekman, P., and Jager, O. (1993) Analyt. Biochem., 214, 138-141.
Usanov, S. A., Chernogolov, A. A., Petrashin, A. I., Akhrem, A. A., and Chashchin, V. L. (1987) Biol. Membr. (Moscow), 4, 1102-1115.
Okamura, T., John, M. E., Zuber, M. X., Simpson, E. R., and Waterman, M. R. (1985) Proc. Natl. Acad. Sci. USA, 82, 5705-5709.
Chashchin, V. L., Lapko, V. N., Adamovich, T. B., Kirillova, N. M., Lapko, A. G., and Akhrem, A. A. (1986) Bioorg. Khim., 12, 1286-1289.
Hiwatashi, A., Sakihama, N., Shin, M., and Ichikawa, Y. (1986) FEBS Lett., 209, 311-315.
Sakihama, N., Hiwatashi, A., Miyatake, A., Shin, M., and Ichikawa, Y. (1988) Arch. Biochem. Biophys., 264, 23-29.
Lobanov, N. A., Vlasova, T. M., Adamovich, T. B., Usanov, S. A., and Chashchin, V. L. (1990) in Proc. VIII Int. Symp. on Microsomes and Drug Oxidations (Ingelman-Sundberg, M., et al., eds.) Karolinska Institutet, Stockholm, pp. 135-136.
Monnier, N., Defaye, G., and Chambaz, E. M. (1987) Eur. J. Biochem., 169, 147-153.
Nemani, R., Ghazarian, J. G., Moorthy, B., Wongsurawat, N., Strong, R., and Armbrecht, H. J. (1989) J. Biol. Chem., 264, 15361-15366.
Driskoll, W. J., and Omdahl, J. L. (1989) Eur. J. Biochem., 185, 181-187.
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Lobanov, N.A., Vlasova, T.M., Adamovich, T.B. et al. Primary Structure of Ferredoxin from Bovine Kidney Mitochondria. Biochemistry (Moscow) 66, 860–864 (2001). https://doi.org/10.1023/A:1011948601816
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DOI: https://doi.org/10.1023/A:1011948601816