Structural modifications of oxidized insulin B-chain induced by glycerol addition

Letters in Peptide Science

Volumn 4, Issue 4-6, 1997, Pages 489-495

  Dupradeau, François Yves ^a   Le Flem, Guillaume ^a   Wieruszeski, Jean Michel ^b   Dauchez, Manuel ^c   Alix, Alain ^c   Larreta Garde, Véronique ^d   Monti, Jean Pierre ^a  

^a UNIVERSITÉ DE PICARDIE JULES VERNE   (France)

^b INSTITUT PASTEUR DE LILLE   (France)

^c Lab Spectroscopies Struct B   (France)

^d Université de Technologie de Compiègne   (France)

Author keywords

CD; Endopeptidase; Micro environment; NMR; Subtilisin BPN

Indexed keywords

EID: 0344579008     PISSN: 09295666     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF02442922     Document Type: Article

References (26)

1. Matsubara, H. and Feder, J., In Boyer, P. (Ed.) The Enzymes, 3rd ed., Vol. 3, Academic Press, New York, NY, U.S.A., 1971, pp. 721-795.
2. Andersson, E. and Han-Hagerdal, B., Biochim. Biophys. Acta, 912 (1987) 317.
3. Larreta-Garde, V., Xu, Z., Lamy, L., Mathlouthi, M. and Thomas, D., Biochem. Biophys. Res. Commun., 155 (1988) 816.
4. Quiocho, F., Wilson, D. and Vyas, N., Nature, 340 (1989) 404.
5. Zaks, A. and Klibanov, A., J. Biol. Chem., 263 (1988) 3194.
6. Russel, A. and Klibanov, A., J. Biol. Chem., 263 (1988) 11624.
7. Watterson, J., Biochem. J., 248 (1987) 615.
8. Hertmanni, P., Picque, E., Thomas, D. and Larreta-Garde, V., FEBS Lett., 279 (1991) 123.
9. Bowski, L., Saini, R., Ryu, D.Y. and Vieth, W., Biotechnol. Bioeng., 23 (1971) 641.
10. Hinsch, B. and Kula, M. R., Biochim. Biophys. Acta, 525 (1978) 392.
11. Lamy, L., Portmann, M.O., Mathlouthi, M. and Larreta-Garde, V., Biophys. Chem., 36 (1990) 71.
12. Kline, A.D. and Justice Jr., R.M., Biochemistry, 29 (1990) 2906.
13. Hua, Q.-X. and Weiss, M.A., Biochim. Biophys. Acta, 1078 (1991) 101.
14. Knegtel, R.M.A., Boelens, R., Ganadu, M.L. and Kaptein, R., Eur. J. Biochem., 202 (1991) 447.
15. Hua, Q.-X. and Weiss, M.A., Biochemistry, 30 (1991) 5505.
16. Olsen, B.H., Ludvigsen, S. and Kaarsholm, N.C., Biochemistry, 35 (1996) 8836.
17. Blundell, T.L., Cutfield, J.F., Cutfield, S.M., Dodson, E.J., Dodson, G.G., Hodgkin, D.C., Mercola, D.A. and Vijayan, M., Nature, 231 (1971) 506.
18. Jorgensen, A.M.M., Olsen, H.B., Balscmidt, P. and Led, J.J., J. Mol. Biol., 257 (1996) 684.
19. Jacoby, E., Hua, Q.-X., Stern, A.S., Frank, B.H. and Weiss, M.A., J. Mol. Biol., 258 (1996) 136.
20. Hua, Q.-X., Sci. China, 32 (1989) 948.
21. Du, Y.-C., Minasiau, E., Treagear, G.W. and Leach, S.J., Int. J. Pept. Protein Res., 20 (1982) 47.
22. Hawkins, B., Cross, K. and Craik, D., Int. J. Pept. Protein Res., 46 (1995) 424.
23. Piotto, M., Saudek, V. and Sklenar, V., J. Biomol. NMR, 2 (1992) 661.
24. Nikiforovich, G.V., Prakash, O., Gehrig, L.A. and Hruby, V.J., J. Am. Chem. Soc., 115 (1993) 3399.
25. Brünger, A.T., Clore, G.M., Gronenborn, A.M., Saffrich, R. and Nilges, M., Science, 261 (1993) 328.
26. Wüthrich, K., NMR of Proteins and Nucleic Acids, Wiley & Sons, New York, NY, U.S.A., 1986.