Abstract
From the liver of fish Dasyatis akajei, ferritin has been isolated by thermal denaturation and ammonium sulfate fractionation and then further purified by anion exchange chromatography and gel exclusion chromatography. The molecular weight of the liver ferritin of D. akajei (DALF) was measured to be 400 kDa by PAGE. Moreover, SDS-PAGE experimentation indicates that protein shell of DALF consists of the H and L subunits with molecular weight of 18 and 13 kDa, respectively. Using isoelectric focusing with pH ranging from 5.0 to 6.0, the ferritin purified by the PAGE exhibited three bands with different pI values in the gel slab. Diameters of the protein shell and iron core were also investigated by transmission electron microscope and determined to be 10–12 nm and 5–8 nm, respectively. A kinetic study of DALF reveals that the rate of self-regulation of the protein shell rather than the complex surface of the iron core plays an important role in forming a process for iron release with mixed orders.
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Andrews, S. C., Arosio, P., Bottke, W., Briat, J. F., von Darl, M., Harrision, P. M., et al. (1992). J. Inorg. Biochem. 47: 161–174.
Arosio, P. A., and Catti, G. (1983). Biochim. Biophys. Acta 744: 230–232.
Bulen, W. A., LeComte, R., and Lough, S. (1973). Biochem. Biophys. Res. Commun. 54: 1274–1281.
Chasteen, N. D. (1998). In: Metal Ions in Biological Systems (Sigel, A., and Digel, H., eds.), Marcel Dekker, Inc., New York, pp. 479–514.
Cheng, Y. G., and Chasteen, N. D. (1991). Biochemistry 30: 2947–2953.
Cooper, T. (1977). Tools of Biochemistry, John Wiley and Sons, New York, pp. 53.
Ford, G. C., Harrison, P. M., and Rice, D. W. (1984). Philos. Trans. R. Soc. Lond. B 304: 551–565.
Funk, F., Lenders, J. P., Crichton, R. P., and Schneider, W. (1985). Eur. J. Biochem. 152: 167–172.
Geetha, C., and Deshpande, V. (1999). Comp. Biochem. Physiol. B 123: 285–294.
Goto, F., and Yoshihara, T. (2001). Plant Biotechnol. 18: 7–15.
Goto, F., Yoshihara, T., and Saiki, H. (2000). Theor. Appl. Genet. 100: 658–664.
Harrison, J. R. (1982). Micron 13: 147–168.
Harrison, P. M., and Arosio, P. (1996). Biochim. Biophys. Acta 1275: 161–203.
Harrison, P. M., Hoy, I. G., Macara, I. G., and Hoare, R. J. (1974). Biochem. J. 143: 445–451.
Harrison, P. M., Treffry, A., and Lilley, T. H. (1986). J. Inorg. Biochem. 27: 287–293.
Huang, H. Q., Watt, R. K., Frankel, R. B., and Watt, G. D. (1993). Biochemistry 32: 1681–1687.
Huang, H. Q., Zhang, F. Z., Chen, Q. H., Qiu, X. F., Xu, L. S., and Zeng, D. (1996). Acta Biochim. Biophys. Sinica 12: 33–37.
Huang, H. Q., Lin, Q. M., Kong, B., Zeng, R. Y., Qiao, Y. H., Chen, C. H., et al. (1999). J. Protein Chem. 18: 497–504.
Huang, H. Q., Xu, L. S., Zhang, F. Z., Qiu, X. F., Lin, Q. M., Huang, J. W., et al. (1998). J. Protein Chem. 17: 45–53.
Huang, H. Q., Lin, Q. M., and Lou, Z. B. (2000). J. Protein Chem. 19: 441–447.
Huang, H. Q., Kong, B., Lin, Q. M., and Cao, T. M. (2002a). Acta Biochim. Biophys. Sinica 18: 99–103.
Huang, H. Q., Lin, Q. M., and Wang, T. L. (2002b). Biophys. Chem. 97: 17–27.
Jacobs, D. L., Watt, G. D., Frankel, R. B., and Papaefthymiou, G. C. (1989). Biochemistry 28: 1650–1655.
Jones, T., Spencer, R., and Walsh, C. (1978). Biochemistry 17: 4011–4017.
Johnson, J. L., Norcross, C. D., Arosio, P., Frankel, R. B., and Watt, G. D. (1999). Biochemistry 38: 6706–6713.
Kadir, F. H. A., Massad, F. K. A., and Moore, G. R. (1992). Biochem. J. 282: 867–870.
Kadir, F. H. A., and Moore, G. R. (1990). FEBS Lett. 276: 81–84.
Laulhere, J. P., Lescure, A. M., and Briat, J. F. (1988). J. Biol. Chem. 263: 10289–10294.
Leong, L. M., Tang, B. H., and Ho, K. K. (1992). Anal. Biochem. 207: 317–320.
Lowry, O. H. (1951). J. Biol. Chem. 193: 265–275.
Mann, S., Bannister, J. V., and Willians, R. J. P. (1986). J. Mol. Biol. 188: 225–232.
Masuda, T., Goto, F., and Yoshihara, T. (2001). J. Biol. Chem. 276: 19575–19579.
Miguel, J. L., Pablos, M. I., and Agapito, M. T. (1991). Biochem. Cell Biol. 69: 735–741.
Otsuka, S., Maruyama, H., and Listowsky, I. (1981). Biochemistry 20: 5226–5232.
Passaniti, A., and Roth, T. F. (1989). Biochem. J. 258: 413–419.
Richards, T. D., Pitts, K. R., and Watt, G. D. (1996). J. Inorg. Biochem. 61: 1–13.
Rohrer, J. S., Islam, Q. T., Watt, G. D., Sayers, D. E., and Theil, E. C. (1990). Biochemistry 29: 259–264.
Sirivech, S., Frieden, E., and Osaki, S. (1974). Biochem. J. 143: 311–315.
Theil, E. C. (1987). Annu. Rev. Biochem. 56: 289–315.
Treffry, A., Bauminger, E. R., Hechel, D., Hodson, N. W., Nowik, I., Ywwdall, S. J., et al. (1993). Biochem. J. 296: 721–728.
Treffry, A., Harrison, P. M., Cleton, M. I., de Bruijnm, W., and Mann, S. (1987). J. Inorg. Biochem. 31: 1–6.
Watt, G. D., Frankel, R. B., Papaefthymiou, G. C., Spartalian, K., and Stiefel, E. I. (1986). Biochemistry 25: 4330–4336.
Watt, G. D., Jacobs, D., and Frankel, R. B. (1988). Proc. Natl. Acad. Sci. USA 85: 7457–7461.
Watt, G. D., Mcdonald, J. W., Chiu, C. H., and Reddy, K. R. N. (1992). J. Inorg. Biochem. 51: 745–750. —-
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Kong, B., Huang, HQ., Lin, QM. et al. Purification, Electrophoretic Behavior, and Kinetics of Iron Release of Liver Ferritin of Dasyatis akajei. J Protein Chem 22, 61–70 (2003). https://doi.org/10.1023/A:1023019911749
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DOI: https://doi.org/10.1023/A:1023019911749