Mass-spectrometric identification of binding proteins of Mr 25,000 protein, a part of vitellogenin B1, detected in particulate fraction of Xenopus laevis oocytes

Protein Journal

Volumn 23, Issue 7, 2004, Pages 467-473

  Sugimoto, Isamu ^a   Li, Zhijun ^b   Yoshitome, Satoshi ^a   Ito, Susumu ^b   Hashimoto, Eikichi ^a  

^a TOTTORI UNIVERSITY   (Japan)

^b JAPAN AGENCY FOR MARINE EARTH SCIENCE AND TECHNOLOGY   (Japan)

Author keywords

Binding protein; Mass spectrometry; Phosphorylated protein; Ribosomal protein; Xenopus laevis oocytes

Indexed keywords

BINDING PROTEIN; RIBOSOME PROTEIN; SERINE; SERINE PROTEINASE INHIBITOR; VITELLOGENIN;

ARTICLE; CELL LYSATE; CLUSTER ANALYSIS; CYTOPLASM; ENDOPLASMIC RETICULUM; FEMALE; MASS SPECTROMETRY; MOLECULAR WEIGHT; NONHUMAN; OOCYTE; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN FUNCTION; PROTEIN PHOSPHORYLATION; PROTEIN SYNTHESIS; PURIFICATION; XENOPUS LAEVIS; ANIMAL; CHEMISTRY; METABOLISM;

ANIMALS; CYTOPLASM; ENDOPLASMIC RETICULUM; MASS SPECTROMETRY; MOLECULAR WEIGHT; OOCYTES; PROTEIN BINDING; VITELLOGENINS; XENOPUS LAEVIS;

EID: 16244408010     PISSN: 15723887     EISSN: 18758355     Source Type: Journal    
DOI: 10.1007/s10930-004-5223-0     Document Type: Article

References (23)

1. Ariizumi, T. and Asashima, M. (2001). Int. J. Dev. Biol. 45: 273-279.
2. Beck, B. L., Henjum, D. C., Antonijczuk, K., Zaharia, O., Korza, G., Ozols, J., et al. (1992). Res. Commun. Chem. Pathol. Pharmacol. 77: 3-16.
3. Bradford, M. M. (1976). Anal. Biochem. 72: 248-254.
4. Ducret, A., Van Oostveen, I., Eng, J. K., Yates, J. R., III, and Aebersold, R. (1998). Protein Sci. 7: 706-719.
5. Funami, J., Miyoshi, N., Sugimoto, I., and Hashimoto, E. (2002). J. Biochem. Mol. Biol. Biophys. 6: 107-111.
6. Goto, N., Muto, S., Sugimoto, I., Ikawa-Kitayama, K., Igarashi, K., Ito, S., and Hashimoto, E. (2001). J. Biochem. 129: 229-236.
7. Hashimoto, E., Takeuchi, F., Tanaka, Y., and Yamamura, H. (1995). J. Biochem. 118: 453-460.
8. Holland, L. J., Suksang, C., Wall, A. A., Roberts, L. R., Moser, D. R., and Bhattacharya, A. (1992). J. Biol. Chem. 267: 7053-7059.
9. Holland, L. J. and Wangh, L. J. (1987). Mol. Cell. Endocrinol. 49: 63-73.
10. Keiper, B. D. and Wormington, W. M. (1990). J. Biol. Chem. 265: 19397-19400.
11. Laemmli, U. K. (1970). Nature 227: 680-685.
12. Radomski, N. and Jost, E. (1995). Exp. Cell Res. 220: 434-445.
13. Shevehenko, A., Wilm, M., Vorm, O., and Mann, M. (1996). Anal. Chem. 68: 850-858.
14. Sugimoto, I. and Hashimoto, E. (2002). Biomed. Res. 23: 187-198.
15. Sunderman, F. W., Jr., Varghese, A. H., Kroftova, O. S., Grbac-Ivankovic, S., Kotyza, J., Datta, A. K., et al. (1996). Mol. Reprod. Dev. 44: 507-524.
16. Wallace, R. A. (1963). Biochim. Biophys. Acta 74: 505-518.
17. Wallace, R. A. and Dumont, J. N. (1968). J. Cell. Phys. 72 (suppl.): 73-89.
18. Washburn, M. P., Wolters, D., and Yates, J. R., III (2001). Nature Biotechnol. 19: 242-247.
19. Wool, I. G. (1979). Annu. Rev. Biochem. 48: 719-754.
20. Xi, J., Sugimoto, I., Yoshitome, S., Yasuda, H., Ogura, K., Mori, N., et al. (2003). J. Protein Chem. 22: 571-583.
21. Yasokawa, M., Sugimoto, I., Fukuma, M., Goto, N., Kobayashi, N., Yasuda, H., et al. (1999). FEBS Lett. 463: 317-320.
22. Yoshitome, S., Furuno, N., Hashimoto, E., and Sagata, N. (2003a). Mol. Cancer Res. 1: 589-597.
23. Yoshitome, S., Nakamura, H., Nakajo, N., Okamoto, K., Sugimoto, I., Kohara, H., et al. (2003b). Dev. Growth Differ. 45: 283-294.