Differential scanning calorimetry and fluorescence study of lactoperoxidase as a function of guanidinium-HCl, urea, and pH

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1804, Issue 7, 2010, Pages 1508-1515

  Zelent, Bogumil ^a   Sharp, Kim A ^a   Vanderkooi, Jane M ^a  

^a UNIVERSITY OF PENNSYLVANIA   (United States)

Author keywords

Denaturation; Protein stability

Indexed keywords

GUANIDINE; LACTOPEROXIDASE; UREA;

ARTICLE; CONCENTRATION (PARAMETERS); CONFORMATIONAL TRANSITION; DIFFERENTIAL SCANNING CALORIMETRY; ENZYME DENATURATION; ENZYME STABILITY; ENZYME STRUCTURE; FLUORESCENCE ANALYSIS; HIGH TEMPERATURE; PH; PRIORITY JOURNAL; THERMOSTABILITY;

ANIMALS; CALORIMETRY; CALORIMETRY, DIFFERENTIAL SCANNING; CATTLE; GUANIDINE; HYDROCHLORIC ACID; HYDROGEN-ION CONCENTRATION; KINETICS; LACTOPEROXIDASE; MICROSCOPY, FLUORESCENCE; MOLECULAR CONFORMATION; TEMPERATURE; THERMODYNAMICS; TRYPTOPHAN; UREA;

BOVINAE;

EID: 77952323466     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2010.03.003     Document Type: Article

References (37)

1. Paul K.G., Ohlsson P.I., and Henriksson A. The isolation and some liganding properties of lactoperoxidase. FEBS Lett. 110 (1980) 200-204
2. Clem W.H., and Klebanoff S.J. Inhibitory effect of saliva on glutamic acid accumulation by Lactobacillus acidophilus and the role of the lactoperoxidase-thiocyanate system. J. Bacteriol. 91 (1966) 1848-1853
3. Stenfors L. Non-specific and specific immunity to bacterial invasion of the middle ear cavity. Int. J. Pediatr. Otorhinolaryngol. 49 (1999) S223-S226
4. Gerson C., Sabater J., Scuri M., Torbati A., Coffey R., Abraham J.W., Lauredo I., Forteza R., Wanner A., Salathe M., Abraham W.M., and Conner G.E. The lactoperoxidase system functions in bacterial clearance of airways. Am. J. Respir. Cell Mol. Biol. 22 (2000) 665-671
5. Kussendrager K.D., and van Hooijdank A.C.M. Lactoperoxidase: physico-chemical properties, occurrence, mechanism of action and applications. Br. J. Nutr. 84 supplement 1 (2000) 19-25
6. Davies M.J., Hawkins C.L., Pattison D.I., and Rees M.D. Mammalian heme peroxidases: from molecular mechanisms to health implications. Antioxid. Redox Signal. 10 (2008) 1199-1234
7. Cals M.M., Mailliart P., Brignon G., Anglade P., and Dumas B.R. Primary structure of bovine lactoperoxidase, a fourth member of a mammalian heme peroxidase family. Eur. J. Biochem. 198 (1991) 733-739
8. Rae T.D., and Goff H.M. The heme prosthetic group of lactoperoxidase. Structural characteristics of heme 1 and heme 1-peptides. J. Biol. Chem. 273 (1998) 27968-27977
9. Singh A.K., Singh N., Sharma S., Singh S.B., Kaur P., Bhushan A., Srinivasan A., and Singh T.P. Crystal structure of lactoperoxidase at 2.4 A resolution. J. Mol. Biol. 376 (2008) 1060-1075
10. Sánchez-Ruiz J.M., López-Lacomba J.L., Cortijo M., and Mateo P.L. Differential scanning calorimetry of the irreversible thermal denaturation of thermolysin. Biochemistry 27 (1988) 1648-1652
11. Lumry R., and Eyring H. Conformation changes of proteins. J. Phys. Chem. 58 (1954) 110-120
12. Sánchez-Ruiz J.M. Theoretical analysis of Lumry-Eyring models in differential scanning calorimetry. Biophys. J. 61 (1992) 921-935
13. Boscolo B., Leal S.S., Ghibadi E.M., and Gomes C.M. Lactoperoxidase folding and catalysis relies on the stabilization of the α-helix rich core domain: a thermal unfolding study. Biochem. Biophys. Acta 1774 (2007) 1164-1172
14. Sturtevant J.M. Biochemical applications of differential scanning calorimetry. Annu. Rev. Phys. Chem. 38 (1987) 463-488
15. Cooper A. Heat capacity effects in protein folding and ligand binding: a re-evaluation of the role of water in biomolecular thermodynamics. Biophys. Chem. 115 (2005) 89-97
16. Konev S.V. Fluorescence and Phosphorescence of Proteins and Nucleic Acids (1967), Plenum Press, New York, NY 9-11
17. Boscolo B., Leal S.S., Salgueiro C.A., Ghibaudi E.M., and Gomes C.M. The prominent conformational plasticity of lactoperoxidase: a chemical and pH stability analysis. Biochim. Biophys. Acta 1794 (2009) 1041-1048
18. Miroliaei M., Nayeri H., Samsam-Shariat S.Z., and Atar A.M. Biospecific immobilization of lactoperoxidase on Con A-Sepharose 4B. Sientia Iranica 14 (2007) 303-307
19. Ciaccio C., De Sanctis G., Marini S., Sinibaldi F., Santucci R., Arcovito A., Bellelli A., Ghibaudi E.M., Roas P.F., and Coletta M. Proton linkage of CO binding and redox properties of bovine lactoperoxidase. Biophys. J. 86 (2004) 448-454
20. Tayefi-Nasrabadi H., and Asadpour R. Effect of heat treatment on buffalo (Bubalus bubalis) lactoperoxidase activity in raw milk. J. Biol. Sci. 8 (2008) 1310-1315
21. Haifeng L., Yuwen L., Xiaomin C., Shiyong W., and Cunxin W. Effects of sodium phosphate buffer on horseradish peroxidase thermal stability. J. Therm. Anal. Calorim. 93 (2008) 569-574
22. McEldoon J.P., and Dordick J.S. Unusual thermal stability of soybean peroxidase. Biotechnol. Prog. 12 (1996) 555-558
23. Pina D.G., Shnyrova A.V., Gavilanes F., Rodriguez A., Leal F., Roig M.G., Sakharov I.Y., Zhadan G.G., Villar E., and Shnyrov V.L. Thermally induced conformational changes in horseradish peroxidase. Eur. J. Biochem. 268 (2001) 120-126
24. Tanford C. The hydrophobic effect and the organization of living matter. Science 200 (1978) 1012-1019
25. Dill K.A. Dominant forces in protein folding. Biochemistry 29 (1990) 7134-7155
26. Cooper A. Heat capacity of hydrogen-bonded networks: an alternative view of protein folding thermodynamics. Biophys. Chem. 85 (2000) 25-39
27. Scott J.N., Nucci N.V., and Vanderkooi J.M. Changes in water structure induced by the guanidinium cation and implications for protein denaturation. J. Phys. Chem. A 112 (2008) 10939-10948
28. Nozaki Y., and Tanford C. The solubility of amino acids, diglycine, and triglycine in aqueous guanidine hdrochloride solutions. J. Biol. Chem. 245 (1970) 1648-1652
29. Venkatesu P., Lee M.J., and Lin H.M. Thermodynamic characterization of the osmolyte effect on protein stability and the effect of GdnHCl on the protein denatured state. J. Phys. Chem. B 111 (2007) 9045-9056
30. Sharp K.A., Madan B., Manas E.S., and Vanderkooi J.M. Water structure changes induced by hydrophobic and polar solutes revealed by simulations and infrared spectroscopy. J. Chem. Phys. 114 (2001) 1791-1796
31. Rezus Y.L.A., and Bakker H.J. Effect of urea on the structural dynamics of water. Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 18417-18420
32. Klotz I.M., and Franzen J.S. Hydrogen bonds between model peptide groups in solution. J. Am. Chem. Soc. 84 (1962) 3461-3466
33. Wetlaufer D.B., Malik S.K., Stoller L., and Coffin R.L. Nonpolar group participation in the denaturation of proteins by urea and guanidinium salts. Model compound studies. J. Am. Chem. Soc. 86 (1964) 508-514
34. Vanderkooi J.M., and Erecinska M. Cytochrome c interaction with membranes. Absorption and emission spectra and binding characteristics of iron-free cytochrome c. Eur. J. Biochem. 60 (1975) 199-207
35. Smith M.L., Paul J., Ohlsson P.-I., Hjortsberg K., and Paul K.G. Heme-protein fission under nondenaturing conditions. Proc. Natl. Acad. Sci. U. S. A. 88 (1991) 882-886
36. Varhac R., Antalik M., and Bano M. Effect of temperature and guanidine hydrochloride on ferrocytochrome c at neutral pH. J. Biol. Inorg. Chem. 9 (2004) 12-22
37. Zelent B., Yano T., Ohlsson P.-I., Smith M.L., Paul J., and Vanderkooi J.M. Optical spectra of lactoperoxidase as a function of solvent. Biochemistry 44 (2005) 15953-15959