Modulation of stability properties of bovine trypsin after in vitro structural changes with a variety of chemical modifiers

Protein Engineering

Volumn 11, Issue 8, 1998, Pages 691-698

  Venkatesh, R ^a   Sundaram, P V ^a  

^a The Voluntary Health Services Chennai   (India)

Author keywords

Chemical modification; Protein structure function; Thermal inactivation; Trypsin

Indexed keywords

GLUTARALDEHYDE; POLYMER; SUCROSE; TRYPSIN; UREA;

ARTICLE; CATTLE; CONTROLLED STUDY; ENTHALPY; ENZYME INACTIVATION; ENZYME MODIFICATION; ENZYME STABILITY; FLUORESCENCE; HALF LIFE TIME; NONHUMAN; PRIORITY JOURNAL; STRUCTURE ACTIVITY RELATION;

BOS TAURUS; BOVINAE;

EID: 0031815023     PISSN: 02692139     EISSN: None     Source Type: Journal    
DOI: 10.1093/protein/11.8.691     Document Type: Article

References (32)

1. Bradford, M. (1976) Anal. Biochem., 72, 248-255.
2. Chaplin, M.F and Bucke, C. (1990) Enzyme Technology. Cambridge University Press, pp. 86-87.
3. Eijsink, V.G.H., Vriend, G., Van den Burg, B., Venema, G. and Stulp, K. (1990) Protein Engng, 4, 99-104.
4. Eijsink, V.G.H., Vriend, G., Van den Burg, B., Van der Zee, R. and Venema, G. (1992) Protein Engng, 5, 165-170.
5. Fassina, G., Vita, C., Dalzoppo, D., Zamai, M., Zambonin, M. and Fontana, A. (1986) Eur. J. Biochem., 156, 221-228.
6. Frigerio, F., Margarit, I., Nogarotto, R., Vincenzode Flippis and Grandi, G. (1996) Protein Engng, 9, 439-445.
7. Geiger, R. and Fritz, H. (1988) In Bergmeyer, H.V. (ed.), Methods of Enzymatic Analysis, Vol. 5. VCH, Verlagsgell. Schaft.mbh, pp. 119-122.
8. Henley, J.P. and Sadana, A. (1985) Enzyme Microb. Technol., 7, 50-60.
9. Kunitz, M. (1947) J. Gen. Physiol., 30, 291-310.
10. Lumry, R. and Eyring, H. (1954) J. Phys.Chem., 58, 110-120.
11. Maeda, Y., Yamada, H., Ueda, T. and Imoto, T. (1996) Protein Engng, 9, 461-465.
12. Marshall, J.J. (1978) Trends Biochem. Sci., 3, 79-81.
13. Mozhaev, V.V., Siksnis, V.A., Merlik-Nubarov, N.S. Galkantaite, N.S., Denis, G.J., Butkis, P., Zaslavsky, B.Y., Mestechkina, N.M. and Martinek, K., (1988) Eur. J. Biochem., 173, 147-154.
14. Mozhaev, V.V. (1993) Trends Biotechnol., 11, 88-95.
15. Nagarajan, V., Pattabhi, V., and Sundaram, P.V. (1996) Ann. N.Y. Acad. Sci., 799, 413-417.
16. Pace, C.N. and Barrett, A.J. (1984) Biochem. J., 219, 411-417.
17. Perutz, M.F. (1978) Science, 201, 1187-1191.
18. Rajalakshmi, N. and Sundaram, P.V. (1995) Protein Engng, 8, 1043-1047.
19. Ray, W.J., Jr and Koshland, D.E., Jr (1961) J. Biol. Chem., 236, 1973-1979.
20. Schmid, R.D. (1979) Adv. Biochem. Engng, 12, 41-118.
21. Schwert, G.W. and Takenaka, Y. (1955) Biochem. Biophys. Acta., 16, 570-575.
22. Sundaram, P.V and Venkatesh, R. (1998) Protein Engng, accompanying paper.
23. Synder, S.L. and Sabocinsky, P.Z. (1975) Anal. Biochem., 64, 284-288.
24. Tanford, C. (1968) Adv. Protein Chem., 23, 122-282.
25. Tor, R., Dror, Y. and Freeman, A. (1989) Enzyme Microb. Technol., 11, 306-312.
26. Tsou, C.L. (1993) Science, 262, 380-381.
27. Van den Burg, B., Dijkstra, B.W., Dervinne, B.V., Stulp, B.K., Eijsink, V.G.H. and Venema, G. (1993) Protein Engng, 6, 521-527.
28. Venkatesh, R., Rajalakshmi, N., Sivakumar, J., Sellers, P. and Sundaram, P.V. (1996) Ann. N.Y. Acad. Sci., 799, 571-576.
29. Voordouw, G., Milo, C. and Roche, R.S. (1976) Biochemistry, 15, 3716-3723.
30. Whistler, R.C. and Bemiller, J.N. (1972) In Whistler, R.A. and Bemiller, J.N. (eds), Methods in Carbohydrate Chemistry, Vol. 1. Academic Press, NY, London, pp. 87-90.
31. Wong, S. (1991) Chemistry of Protein Conjugation and Cross-linking. CRC Press, Boca Raton, Boston, Ann Arbor, London, pp. 101-102.
32. Wong, S.S. and Wong, L.J.J (1992) Enzyme Microb. Technol., 14, 866-874.