Effect of polyethylene glycols on the function and structure of thiol proteases

Journal of Biochemistry

Volumn 142, Issue 1, 2007, Pages 65-72

  Fatima, Sadaf ^a   Khan, Rizwan Hasan ^a  

^a ALIGARH MUSLIM UNIVERSITY   (India)

Author keywords

Poly(ethylene glycol); Protein stability; Synthetic substrate; Thiol proteases

Indexed keywords

ACRYLAMIDE; BROMELAIN; CHYMOPAPAIN; MACROGOL; MACROGOL 20000; MACROGOL 400; MACROGOL 6000; PAPAIN; THIOL PROTEINASE; TRYPTOPHAN; 8 ANILINO 1 NAPHTHALENESULFONIC ACID; 8-ANILINO-1-NAPHTHALENESULFONIC ACID; CYSTEINE PROTEINASE; MACROGOL DERIVATIVE; UNCLASSIFIED DRUG;

ARTICLE; CIRCULAR DICHROISM; PROTEIN DEGRADATION; PROTEIN FUNCTION; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; PROTEIN STRUCTURE; BINDING SITE; CHEMISTRY; HYDROPHOBICITY; METABOLISM; MOLECULAR WEIGHT; PROTEIN DENATURATION; PROTEIN FOLDING; SPECTROFLUOROMETRY; STRUCTURE ACTIVITY RELATION; TEMPERATURE;

ACRYLAMIDE; ANILINO NAPHTHALENESULFONATES; BINDING SITES; BROMELAINS; CHYMOPAPAIN; CIRCULAR DICHROISM; CYSTEINE ENDOPEPTIDASES; HYDROPHOBICITY; MOLECULAR WEIGHT; PAPAIN; POLYETHYLENE GLYCOLS; PROTEIN DENATURATION; PROTEIN FOLDING; SPECTROMETRY, FLUORESCENCE; STRUCTURE-ACTIVITY RELATIONSHIP; TEMPERATURE;

EID: 38449098568     PISSN: 0021924X     EISSN: 17562651     Source Type: Journal    
DOI: 10.1093/jb/mvm108     Document Type: Article

References (22)

1. Pace, N. (1970) Conformational stability of globular proteins. Trends Biochem. Sci. 15, 14-17
2. Walter, H., Brooks, D.E., and Fisher, D. (1985) Theory, methods, uses and applications to biotechnology. in Partitioning in Aqueous Two-Phase System (Walter, H., Brooks, D. E., and Fisher, D., eds.) pp. 324-352 Academic Press, Orlando-FL
3. Abbott, N.L., Blankschtein, D., and Hatton, T.A. (1990) On protein partitioning in two-phase aqueous polymer systems. Bioseparation 1, 191-225
4. McPherson, A. (1999) Crystallization of Biological Macromolecules, Cold Spring Harbor Laboratory Press, Plainview, NY
5. Cohen, L.W., Coghlan, V.M., and Diehl, L.C. (1986) Cloning and sequencing of papain-encoding cDNA. Gene 48, 21-227
6. Watson, D.C., Yaguchi, M., and Lynn, K.R. (1990) The amino acid sequence of chymopapain from Carica papaya. Biochem. J. 266, 75-81
7. Ritonja, A., Rowan, A.D., Buttle, D.J., Rawlings, N.D., Turk, V., and Barett, A.J. (1989) Stem bromelain: amino acid sequence and implications for weak binding of cystatin. FEBS Lett. 247, 419-424
8. Mendiola, S.S., Dominguez, A.R., and Arana, A.H. (1993) Cooperativity in the unfolding transitions of cysteine proteinases, calorimetric study of the heat denaturation of chymopapain and papain. Biochim. Biophys. Acta 1203, 121-125
9. Reyna, A.A. and Arana, A.H. (1995) The thermal denaturation of stem bromelain is consistent with an irreversible two-state model. Biochim. Biophys. Acta 1248, 123-128
10. Eftink, M.R. and Ghiron, C.A. (1982) Fluorescence quenching studies with proteins. Anal. Biochem. 114, 199-227
11. Edwin, F. and Jagannadham, M.V. (1998) Sequential unfolding of papain in molten globule state. Biochem. Biophys. Res. Commun. 252, 654-660
12. Eftink, M.R. (1994) The use of fluorescence methods to monitor unfolding transitions in proteins. Biophys. J. 66, 482-501
13. Drenth, J., Jansonius, J.N., Koekoek, R., Swen, N.M., and Wolthers, B.G. (1968) Structure of papain. Nature 218, 929-935
14. Timasheff, S.N. (1998) Control of protein stability and reactions by weakly interacting cosolvents: the simplicity of the complicated. Adv. Protein Chem. 51, 355-432
15. Bolen, D.W. (2004) Effects of naturally occurring osmolytes on protein stability and solubility: issues important in protein crystallization. Methods 34, 312-322
16. Arakawa, T., Bhat, R., and Timasheff, S.N. (1990) Why preferential hydration does not always stabilize the native structure of globular proteins. Biochemistry 29, 1924-1931
17. Lee, J.C. and Lee, L.L. (1981) Preferential solvent interactions between proteins and polyethylene glycols. J. Biol. Chem. 256, 625-631
18. Lee, J.C. and Lee, L.L. (1979) Interaction of calf brain tubulin with poly(ethylene glycols). Biochemistry 18, 5518-5526
19. Timasheff, S.N. and Inoue, H. (1968) Preferential binding of solvent components to proteins in mixed water-organic solvent systems. Biochemistry 7, 2501-2513
20. Lee, J.C. and Lee, L.L. (1987) Thermal stability of proteins in the presence of poly(ethylene glycols). Biochemistry 26, 7813-7819
21. Arakawa, T. and Timasheff, S.N. (1985) Mechanism of poly(ethylene glycol) interaction with proteins. Biochemistry 24, 6756-6762
22. Pace, C.N. and Marshal, H.F. (1980) A comparison of the effectiveness of protein denaturants for beta-lactoglobulin and ribonuclease. Arch. Biochem. Biophys. 199, 270-276