Urea-induced denaturation of β-trypsin: An evidence for a molten globule state

Protein and Peptide Letters

Volumn 11, Issue 2, 2004, Pages 133-140

  Nasser Brumano, Maria Helena ^a   De Almeida Oliveira, Maria Goreti ^a  

^a FEDERAL UNIVERSITY OF VIÇOSA   (Brazil)

Author keywords

trypsin; Molten globule state; Urea denaturation

Indexed keywords

5,5' BIS(8 (PHENYLAMINO) 1 NAPHTHALENESULFONATE); 5,5'-BIS(8-(PHENYLAMINO)-1-NAPHTHALENESULFONATE); 8 ANILINO 1 NAPHTHALENESULFONIC ACID; TRYPSIN; UREA;

ANIMAL; ARTICLE; CATTLE; CHEMISTRY; CIRCULAR DICHROISM; ENZYME STABILITY; PH; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; SPECTROFLUOROMETRY;

ANILINO NAPHTHALENESULFONATES; ANIMALS; CATTLE; CIRCULAR DICHROISM; ENZYME STABILITY; HYDROGEN-ION CONCENTRATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SPECTROMETRY, FLUORESCENCE; TRYPSIN; UREA;

ANIMALIA; BOS TAURUS;

EID: 1942456587     PISSN: 09298665     EISSN: None     Source Type: Journal    
DOI: 10.2174/0929866043478257     Document Type: Article

References (19)

1. Aral, M., and Kuwajima, K. (1996) Folding and Design, 1, 275-287.
2. Kumar, T.K.S., Jayaraman, G., Lee, C.-S., Sivaraman, T., Lin, W-L, and Yu, C. (1995) Biochem. Biophys. Res. Comm., 207, 536-543.
3. Iglesias, M.M., Elola, M.T., Martinez, V., Fink, N., and Wolfenstein-Todel, C. (2003) Biochim. Biophys. Acta, 1648, 164-173.
4. Bartunick, H.D., Summers, L.J., and Bartsch, H.H. (1989) J. Mol. Biol., 210, 813-828.
5. Brumano, M.H.N., Rogana, E., and Swaisgood, H.E. (2000) Arch. Biochem. Biophys., 382, 57-62.
6. Ruan, K., Lange, R., Bec, N., and Balny, C. (1997) Biochem. Biophys. Res. Comm., 239, 150-154.
7. Schroeder D.D., and Shaw, E. (1968) J. Biol. Chem., 243, 2943-2949.
8. Erlanger, B.F., Kokowsky, N., Cohen, W. (1961) Arch. Biochem. Biophys. 95, 271-278.
9. Laemmli, U.K. T4. (1970) Nature, 227, 680-685.
10. Chase, T., and Shaw, E. (1967) Biochem. Biophys. Res. Comm., 29, 508-514.
11. Pace, C.N., Shirley B., and Thompson, J. (1990) in Protein Structure: A Practical Approach, (Creighton, T.E., ed.), Oxford, UK: IRL Press.
12. Silva, J.L., Miles, E.W., Weber, G. (1986) Biochemistry, 25, 5780-5786.
13. Otlewski, J., Sywula, A., Kolasinski, M. (1996) Eur. J. Biochem., 242, 601-607.
14. Fujiwara, K., Arai, M., Shimizu, A., Ikeguchi, M., Kuwajima, K., and Sugai, S. (1999) Biochemistry, 38, 4455-4463.
15. Semisotnov, G.V., Rodionova, N.A., Razgulyaev, O.I., Uversky, V.N., Gripas, A.F., and Gilmanshin, R.I. (1991) Biopolymers, 31, 119-128.
16. Lakowicz, J.R. (1983) in Principles of Fluorescence Spectroscopy, Plenum Press, New York.
17. Manavalan, P., and Johnson, W.C. Jr. (1983) Nature, 305, 831-832.
18. Hamada, D., and Goto, Y.J. (1997) J. Mol. Biol., 269, 479-487.
19. Perczel, A., Park, K., Fasman, G.D. (1992) Proteins Struct., Funct. Genet., 13, 57-69.