Temperature and pH sensitivity of trypsins from Atlantic salmon (Salmo salar) in comparison with bovine and porcine trypsin

Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology

Volumn 115, Issue 1, 1996, Pages 33-45

  Outzen, Heidi ^a   Berglund, Gunnar I ^a   Smalås, Arne O ^a   Willassen, Nils P ^a  

^a UNIVERSITY OF TROMSØ   (Norway)

Author keywords

Atlantic salmon; cold adaptation; fish; pH stability; Salmo salar; serine proteinase; temperature stability; trypsin; unfolding

Indexed keywords

ISOENZYME; TRYPSIN;

ADAPTATION; ARTICLE; CATTLE; ENZYME ANALYSIS; FISH; FLUORESCENCE; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN FOLDING; SPECIES DIFFERENCE; SWINE; TEMPERATURE;

BOS TAURUS; BOVINAE; MAMMALIA; SALMO SALAR; SUIDAE; SUS SCROFA;

EID: 0029851195     PISSN: 03050491     EISSN: None     Source Type: Journal    
DOI: 10.1016/0305-0491(96)00081-8     Document Type: Article

References (39)

1. Asgeirsson, B.; Bjarnason, J.B. Structural and kinetic properties of chymotrypsin from Atlantic cod (Gadus morhua). Comparison with bovine chymotrypsin. Comp. Biochem. Physiol. 99B:327-335;1991.
2. Asgeirsson, B.; Bjarnason, J.B. Properties of elastase from Atlantic cod, a cold-adapted proteinase. Biochimica et Biophysica Acta 1164:91-100;1993.
3. Asgeirsson, B.; Fox, J.W.; Bjarnason, J.B. Purification and characterization of trypsin from the poikilotherm Gadus morhua. Eur. J. Biochem. 180:85-94;1989.
4. Berglund, G.I.; Smalås, A.O.; Hordvik, A.; Willassen, N.P. Structure of anionic salmon trypsin in a second crystal form. Acta Cryst. D51;1995, in press.
5. Berglund, G.I.; Smalås, A.O.; Hansen, L. Kr.; Hordvik, A.; Willassen, N.P. Crystallization and preliminary X-ray crystallographic studies of native elastase from North Atlantic salmon (Salmo salar). Acta Cryst. D51;1995.
6. Berglund, G.I.; Smalås, A.O.; Hordvik, A.; Willassen, N.P. Structure of native pancreatic elastase from Atlantic salmon at 1.61 A resolution. Acta Cryst. D51;1995, in press.
7. Chase Jr., T.; Shaw, E. p-Nitrophenyl-p′-guanidinobenzoate HCl: a new active site titrant for trypsin. Biochem. Biophys. Res. Comm. 29:508-514;1967.
8. Eriksson, A.E.; Baase, W.A.; Matthews, B.W. Similar hydrophohic replacements of Leu99 and Phe153 within the core of T4 lysozyme have different structural and thermodynamic consequences. J. Mol. Biol. 229:747-769;1993.
9. Erlanger, B.F.; Kokowsky, N.; Cohen, W. The preparation and properties of two new chromogenic substrates of trypsin. Arch. Biochem. Biophys. 95:271-278;1961.
10. Gildberg, A.; Øverbø, K. Purification and characterization of pancreatic elastase from Atlantic cod (Gadus morhua). Comp. Biochem. Physiol. 97B:775-782;1990.
11. Gudmundsdóttir, A.; Gudmundsdóttir, E.; Óskarsson, S.; Bjarnason, J.B.; Eakin, A.K.; Craik, C.S. Isolation and characterization of cDNAs from Atlantic cod encoding two different forms of trypsinogen. Eur. J. Biochem. 217:1091-1097;1993.
12. Gudmundsdóttir, A.; Oskarsson, S.; Eakin, A.E.; Craik, C.S.; Bjarnason, J.B. Atlantic cod cDNA encoding a psychrophilic chymotrypsinogen. Biochimica et Biophysica Acta 1219:211-214;1994.
13. Haard, N.F. A review of proteolytic enzymes from marine organisms and their application in the food industry. J. Aquatic Food Products Technol. 1:17-35;1992.
14. Hedstrom, L.; Szilagyi, L.; Rutter, W.J. Converting trypsin to chymotrypsin: the role of surface loops. Science 255:1249-1253;1992.
15. Heimstad, E.S.; Hansen, L. Kr.; Smalås, A.O. Comparative molecular dynamics studies of salmon and ho vine trypsins in aqueous solution. Protein Eng. 8;1995.
16. Hjelmeland, K.; Raa, J. Characteristics of two trypsin type isozymes isolated from the Arctic fish capelin (Mallotus villosus). Comp. Biochem. Physiol. 71B:557-562;1982.
17. Hochachka, P.W.; Somero, G.N. Temperature adaptation. In: Biochemical Adaptations. Princeton, New Jersey: Princeton University Press; 1984: chap. 11.
18. Kim, H.R.; Meyers, S.P.; Godher, J.S. Purification and characterization of anionic trypsins from the hepatopancreas of crayfish, Procambarus clarkii. Comp. Biochem. Physiol. 103B:391-398;1992.
19. Kim, H.R.; Meyers, S.P.; Pyeun, J.H.; Godber, J.S. Enzymatic properties of anionic trypsins from the hepatopancreas of crayfish, Procambarus clarkii. Comp. Biochem. Physiol. 107B:197-203;1994.
20. Kristjánsson, M.M.; Nielsen, H.H. Purification and characterization of two chymotrypsin-like proteases from the pyloric caeca of rainbow trout (Oncorhynchus mykiss). Comp. Biochem. Physiol. 101B:247-253;1992.
21. Lazdunski, M.; Delaage, M. Etude structurale du trypsinogéne et de la trypsine. Les diagrammes d'étate. Biochim. Biophys. Acta 140:417-434;1967.
22. Low, P.; Somero, G.N. Temperature adaptation of enzymes: a proposed molecular basis for the different catalytic efficiencies of enzymes from ectotherms and endotherms. Comp. Biochem. Physiol. 49B:307-312;1974.
23. Male, R.; Lorents, J.B.; Smalås, A.O.; Torrissen, K.R. Molecular cloning and characterization of anionic and cationic variants of trypsin from Atlantic salmon. Eur. J. Biochem. 232: 677-685;1995.
24. Martínez, A.; Olsen, R.L.; Serra, J .L. Purification and characterization of two trypsin-like enzymes from the digestive tract ot anchovy Engraulis encrasicholus. Comp. Biochem. Physiol. 91B:677-684;1988.
25. Monera, O.D.; Kay, C.M.; Hodges, R.S. Protein denaturation with guanidinium hydrochloride and urea provides a different estimate of stability depending on the contributions of electrostatic interactions. Protein Science 3:1984-1991;1994.
26. Monera, O.D.; Kay, C.M.; Hodges, R.S. Electrostatic interactions control the parallel and antiparallel orientation of a-helical chains in two-stranded a-helical coiled-coils. Biochemistry 33:3862-3871;1994.
27. Osnes, K. Kr.; Mohr, V. On the purification and characterization of three anionic, serine type peptide hydrolases from Antarctic krill, Euphausia Superba. Comp. Biochem. Physiol. 82B: 607-619;1985.
28. Pace, C.N. Determination and analysis of urea and guanidinium hydrochloride denaturation curves. Methods Enzymol. 131:266-280;1975.
29. Perutz, M.F. Electrostatic effects in proteins. Science 201: 1187-1191;1978.
30. Raae, A.J. Effect of low and high temperatures on chymotrypsin from Atlantic cod (Gadus morhua L.). Comparison with bovine a-chymotrypsin. Comp. Biochem. Physiol. 97B:145-149;1990.
31. Simpson, B.K.; Haard, N.F. Purification and characterization of trypsin from the Greenland cod (Gadus ogac). 1. Kinetic and thermodynamic characteristics. Can. J. Biochem. Cell. Biol. 62:894-900;1984.
32. Simpson, B.K.; Haard, N.F. Trypsin from Greenland cod, Gadus ogac. Isolation and comparative properties. Comp. Biochem. Physiol. 79B:613-622;1984.
33. Smalås, A.O.; Hordvik, A. Structure determination and refinement of benzamidine-inhibited trypsin from the North Atlantic salmon (Salmo salar) at 1.82 Å resolution. Acta Cryst. D49:318-330;1993.
34. Smalås, A.O.; Heimstad, E.S.; Hordvik, A.; Willassen, N.P.; Male, R. Cold adaption of enzymes: structural comparison between salmon and bovine trypsins. Proteins: Structure, Function, and Genetics 20:149-166;1994.
35. Smalås, A.O.; Hordvik, A.; Hansen, L. Kr.; Hough, E.; Jynge, K. Crystallization and preliminary X-ray crystallographic studies of benzamidine-inhibited trypsin from the North Atlantic salmon (Salmo salar). J. Mol. Biol. 214:355-358;1990.
36. Somero, G.N. Temperature as a selective factor in protein evolution: the adaptational strategy ot "compromise". J. Exp. Zool. 194:175-188;1975.
37. Walsh, K.A. Trypsinogens and trypsins of various species. Methods Enzymol. 19:41-63;1970.
38. Yoshinaka, R.; Sato, M.; Suzuki, T.; Ikeda, S. Enzymatic characterization of anionic trypsin of the catfish (Parasilurus asotus). Comp. Biochem. Physiol. 77B:1-6;1984.
39. Zerner, B.; Bender, M.L. The kinetic consequences of the acyl-enzyme mechanism for the reactions of specific substrates with chymotrypsin. J. Am. Chem. Soc. 86:3669-3674;1964.