Influence of limited proteolysis, detergent treatment and lyophilization on the phenoloxidase activity of Rapana thomasiana hemocyanin

International Journal of Biological Macromolecules

Volumn 45, Issue 2, 2009, Pages 181-187

  Idakieva, Krassimira ^a   Siddiqui, Nurul Islam ^b   Meersman, Filip ^b   De Maeyer, Marc ^b   Chakarska, Irena ^a   Gielens, Constant ^b  

^a INSTITUTE OF ORGANIC CHEMISTRY   (Bulgaria)

^b UNIVERSITY OF LEUVEN   (Belgium)

Author keywords

Hemocyanin; Phenoloxidase activity; Rapana thomasiana

Indexed keywords

CATECHOL; CATECHOL OXIDASE; COPPER; DETERGENT; DODECYL SULFATE SODIUM; HEMOCYANIN; MONOPHENOL MONOOXYGENASE; SUBTILISIN;

ARTICLE; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME INDUCTION; FREEZE DRYING; GASTROPOD; INFRARED SPECTROSCOPY; MOLECULAR MODEL; NONHUMAN; PROTEIN DEGRADATION; PROTEIN SECONDARY STRUCTURE;

RAPANA THOMASIANA;

EID: 67349154399     PISSN: 01418130     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ijbiomac.2009.04.022     Document Type: Article

References (24)

1. Solomon E.I., Baldwin M.J., and Lowery M.D. Chem. Rev. 92 (1992) 521-542
2. Solomon E.I., and Lowery M.D. Science 259 (1993) 1575-1581
3. Volbeda A.A., and Hol W.G. J. Mol. Biol. 209 (1989) 249-279
4. Hazes B., Magnus K.A., Bonaventura C., Bonaventura J., Dauter Z., Kalk K.H., and Hol W.G. Protein Sci. 2 (1993) 597-619
5. Cuff M.E., Miller K.I., van Holde K.E., and Hendrickson W.A. J. Mol. Biol. 278 (1998) 855-870
6. Perbandt M., Guthöhrlein E., Rypniewski W., Idakieva K., Stoeva S., Voelter W., Genov N., and Betzel C. Biochemistry 42 (2003) 6341-6346
7. Klabunde T., Eicken C., Sacchettini J., and Krebs B. Nat. Struct. Biol. 5 (1998) 1084-1090
8. Matoba Y., Kumagai T., Yamamoto L., Yoshitsu H., and Sugiyama M. J. Biol. Chem. 281 (2006) 8981-8990
9. Decker H., and Tuczek F. Trends Biochem. Sci. 25 (2000) 392-397
10. Decker H., and Jaenicke E. Dev. Comp. Immunol. (2004) 673-687
11. Salvato B., Santamaria M., Beltramini M., Alzuet G., and Casella L. Biochemistry 37 (1998) 14065-14077
12. Siddiqui N.I., Akosung R.F., and Gielens C. BBRC 348 (2006) 1138-1144
13. Hristova R., Dolashki A., Voelter W., Stevanovic S., and Dolashka-Angelova P. Comp. Biochem. Physiol. B149 (2008) 439-446
14. Baird S., Kelly S., Price N., Jaenicke E., Meesters C., Nillius D., Decker H., and Nairn J. Biochim. Biophys. Acta 1774 (2007) 1380-1394
15. Idakieva K., Severov S., Svendsen I., Genov N., Stoeva S., Beltramini M., Tognon G., Di Muro P., and Salvato B. Comp. Biochem. Physiol. 106B (1993) 53-59
16. Idakieva K., Schwarz H., Genov N., Voelter W., and Stoeva S. Micron 33 (2002) 7-14
17. Stoeva S., Idakieva K., Betzel C., Genov N., and Voelter W. Arch. Biochem. Biophys. 399 (2002) 149-158
18. Delhaise P., Bardiaux M., De Maeyer M., Prevost M., Vanbelle D., Donneux J., Lasters I., Vancustem E., Alard P., and Wodak S.J. J. Mol. Graph. 6 (1988) 219-1219
19. Alard P., and Wodak S.J. J. Comp. Chem. 12 (1991) 918-922
20. Naraoka T., Uchisawa H., Mori H., Matsue H., Chiba S., and Kimura A. Eur. J. Biochem. 270 (2003) 4026-4038
21. Eicken C., Zippel F., Buldt-Karentzopoulos, and Krebs B. FEBS Lett. 436 (1998) 293-299
22. Carpenter J.F., Kendrick B.S., Chang B.S., Manning M.C., and Randolph T.W. Methods Enzymol. 309 (1999) 236-255
23. Yesilyurt B.T., Gielens C., and Meersman F. FEBS J. 275 (2008) 3625-3632
24. Campello S., Beltramini M., Giordano G., Di Muro P., Marino S.M., and Bubacco L. Arch. Biochem. Biophys. 471 (2008) 159-167