Fourier-transform infrared spectroscopic studies on the coordination of the side-chain COO- groups to Ca2+ in equine lysozyme

European Journal of Biochemistry

Volumn 250, Issue 1, 1997, Pages 72-76

  Mizuguchi, Mineyuki ^a   Nara, Masayuki ^b   Ke, Yue ^c   Kawano, Keiichi ^a   Hiraoki, Toshifumi ^a   Nitta, Katsutoshi ^a  

^a HOKKAIDO UNIVERSITY   (Japan)

^b TOKYO MEDICAL AND DENTAL UNIVERSITY   (Japan)

^c INNER MONGOLIA NORMAL UNIVERSITY   (China)

Author keywords

Calcium binding; Coordination type; Equine lysozyme; Fourier transform infrared spectroscopy; lactalbumin

Indexed keywords

ASPARTIC ACID; CALCIUM ION; CARBOXYL GROUP; DIVALENT CATION; LACTALBUMIN; LYSOZYME; METAL ION; WATER;

ARTICLE; BINDING SITE; CALCIUM BINDING; CONTROLLED STUDY; COORDINATION; FOURIER TRANSFORMATION; HORSE; HYDROGEN BOND; INFRARED SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN CONFORMATION;

BOVINAE; EQUIDAE; EQUUS CABALLUS;

EID: 0030834528     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1997.00072.x     Document Type: Article

References (26)

1. Acharya, K. R., Stuart, D. I., Walker, N. P. C., Lewis, M. & Phillips. D. C. (1989) Refined structure of baboon α-lactalbumin at 1.7 Å resolution: comparison with c-type lysozyme, J. Mol. Biol. 208, 99 - 127.
2. Acharya, K. R., Ren, J., Stuart, D. I., Phillips, D. C. & Fenna, R. E. (1991) Crystal structure of human α-lactalbumin at 1.7 Å resolution, J. Mol. Biol. 221, 571 - 581.
3. Aramini, J. M., Drakenberg, T., Hiraoki, T., Yue Ke, Nitta, K. & Vogel, H. J. (1992) Calcium-43 NMR studies of calcium-binding lysozymes and α-lactalbumins, Biochemistry 31, 6761 - 6768.
4. Aramini, J. M., Hiraoki, T., Yue Ke, Nitta, K. & Vogel, H. J. (1995) Cadmium-113 NMR studies of bovine and human α-lactalbumin and equine lysozyme, J. Biochem. (Tokyo) 117, 623 - 628.
5. Bell, K., McKenzie, H. A., Muller, V., Roger, C. & Shaw, D. C. (1981) Equine whey proteins, Comp. Biochem. Physiol. 68B, 225 - 236.
6. Brew, K., Castellino, F. J., Vanaman, T. C. & Hill, R. L. (1970) The complete amino acid sequence of bovine α-lactalbumin, J. Biol. Chem. 245, 4570 - 4582.
7. 2+ to bovine α-lactalbumin and equine lysozyme, J. Inorg. Biochem. 37, 185 - 191.
8. Hiraoka, Y. & Sugai, S. (1985) Equilibrium and kinetic study of sodium-potassium-induced conformational changes of apo-α-lactalbumin, Int. J. Pept. Protein Res. 20, 252 - 261.
9. 2+ binding site, J. Biol. Chem. 266, 20 666 - 20 671.
10. Lin, T. Y. (1970) Lactose synthetase: modification of carboxyl groups, Biochemistry 9, 984 - 995.
11. 2+ -binding site, FEBS Lett., in the press.
12. 2+ -binding proteins: marker hands for identifying the types of coordination of the side-chain COO groups to metal ions in pike parvalbumin (pI = 4.10), FEBS Lett. 349, 84 -88.
13. 2+ on calmodulin by Fourier-transform infrared spectroscopy, Biospectroscopy 1, 47 - 54.
14. Nitta, K., Tsuge, H., Sugai, S. & Shimazaki, K. (1987) The calcium-binding property of equine lysozyme, FEBS Lett. 223, 405 - 408.
15. Nitta, K., Tsuge, H., Shimazaki, K. & Sugai, S. (1988) Calcium-binding lysozymes, Biol. Chem. Hoppe-Seyler 369, 671 - 675.
16. Nitta, K. & Sugai, S. (1989) The evolution of lysozyme and α-lactalbumin, Eur. J. Biochem. 182, 111 - 118.
17. Nitta, K., Tsuge, H. & Iwamoto, H. (1993) Comparative study of the stability of the folding intermediates of the calcium-binding lysozymes, Int. J. Pept. Protein Res. 41, 118 - 123.
18. Qasba, P. K. & Safaya, S. K. (1984) Similarity of the nucleotide sequences of rat α-lactalbumin and chicken lysozyme genes, Nature 308, 377 - 380.
19. Pike, A. C. W., Brew, K. & Acharya, K. R. (1996) Crystal structures of guinea-pig, goat and bovine α-lactalbumin highlight the enhanced conformational flexibility of regions that are significant for its action in lactose synthase, Structure (Lond.) 4, 691 - 703.
20. 10-helices in globular proteins, Int. J. Peptide Res. 37, 508 - 512.
21. Prestrelski, S. J., Byler, D. M. & Thompson M. P. (1991b) Effect of metal ion binding on the secondary structure of bovine α-lactalbumin as examined by infrared spectroscopy, Biochemistry 30, 8797 - 8804.
22. Stuart, D. I., Acharya, K. R., Walker, N. P. C., Smith, S. G., Lewis, M. & Phillips, D. C. (1986) α-Lactalbumin possesses a novel calcium binding loop, Nature 324, 84 - 87.
23. Surewicz, W. K. & Mantsch, H. H. (1988) New insight into protein secondary structure from resolution-enhanced infrared spectra, Biochem. Biophys. Acta 952, 115 - 130.
24. 1H-NMR, Biochem. Biophys. Acta 1078, 77 - 84.
25. Tsuge, H., Ago, H., Noma, M., Nitta, K., Sugai, S. & Miyano, M. (1992) Cristallographic studies of a calcium binding lysozyme from equine milk at 2.5 Å resolution, J. Biochem. (Tokyo) 111, 141 - 143.
26. Van Dael, H., Haezebrouck, P., Monozova, L., Ariko-Muendel, C. & Dobson, C. M. (1993) Partially folded states of equine lysozyme: structual characterization and significance for protein folding. Biochemistry 32, 11 886 - 11 894.