Oxidative refolding of denatured/reduced lysozyme utilizing the chaperone-like function of liposomes and immobilized liposome chromatography

Biotechnology Progress

Volumn 15, Issue 3, 1999, Pages 480-487

  Yoshimoto, Makoto ^a   Kuboi, Ryoichi ^a  

^a OSAKA UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

2 OLEOYL 1 PALMITOYLPHOSPHATIDYLCHOLINE; CHAPERONE; CHROMATOGRAPHY; ENZYME STRUCTURE; IMMOBILIZED LIPOSOME; LIPOSOME; LYSOZYME;

BIOLOGICAL MEMBRANES; CATALYST ACTIVITY; CHEMICAL BONDS; CHROMATOGRAPHY; CONFORMATIONS; ENZYME IMMOBILIZATION; HYDROPHOBICITY; MOLECULAR DYNAMICS; OXIDATION; PHASE SEPARATION; PROTEINS;

ENZYMATIC ACTIVITY; IMMOBILIZED LIPOSOME CHROMATOGRAPHY; LIPOSOMES; LYSOZOME; OXIDATIVE REFOLDING;

ENZYME KINETICS;

EID: 0033006157     PISSN: 87567938     EISSN: None     Source Type: Journal    
DOI: 10.1021/bp990050b     Document Type: Article

References (47)

1. Goldberg, M. E.; Rudolph, R.; Jaenicke, R. A kinetic study of the competition between renaturation and aggregation during the refolding of denatured-reduced egg white lysozyme. Biochemistry 1991, 30, 2790-2797.
2. Raman, B.; Ramakrishna, T.; Rao, Ch. M. Refolding of denatured and denatured/reduced lysozyme at high concentrations. J. Biol. Chem. 1996, 271, 17067-17072.
3. Kuboi, R.; Yoshimoto, M.; Walde, P.; Luisi, P. L. Refolding of carbonic anhydrase assisted by 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine liposomes. Biotechnol. Prog. 1997, 13, 828-836.
4. Yoshimoto, M.; Kuboi, R.; Yang, Q.; Miyake, J. Immobilized liposome chromatography for studies of protein-membrane interactions and refolding of bovine carbonic anhydrase. J. Chromatogr. B 1998, 712, 59-71.
5. Yang, Q.; Liu, X.-Y.; Yoshimoto, M.; Kuboi, R; Miyake, J. Covalent immobilization of unilamellar liposomes in gel beads for chromatography. Anal. Biochem. 1999, 268, 354-362.
6. Hevehan, D.; Clark, E. De B. Oxidative renaturation of lysozyme at high concentration. Biotechnol. Bioeng. 1997, 54, 221-230.
7. Light, A.; Odorzynski, W. Refolding of bovine trypsinogen with one and two disulfide bonds reduced and carboxymethylated. J. Biol. Chem. 1979, 254, 9162-9166.
8. Puig, A.; Gilbert, H. F. Protein disulfide isomerase exhibits chaperone and anti-chaperone activity in the oxidative refolding of lysozyme. J. Biol. Chem. 1994, 269, 7764-7771.
9. Fischer, B. Folding of lysozyme. EXS 1996, 75, 143-161.
10. Uversky, V. N. Use of fast protein size-exclusion liquid chromatography to study the unfolding of proteins which denature through the molten globule. Biochemistry 1993, 32, 13288-13298.
11. Okazaki, A.; Ikura, T.; Nikaido, K.; Kuwajima, K. The chaperone GroEL does not recognize apo-α-lactalbumin in the molten globule state. Struct. Biol. 1994, 1, 439-446.
12. Banuelos, S.; Muga, A. Interaction of native and partially folded conformations of α-lactalbumin with lipid bilayers: characterization of two membrane-bound states. FEBS Lett. 1996, 386, 21-25.
13. Oku, N.; MacDonald, R. C. Differential effects of alkali metal chlorides on formation of giant liposomes by freezing and thawing and dialysis. Biochemistry 1983, 22, 855-863.
14. Bangham, A. D.; Standish, M. M.; Watkins, J. C. Diffusion of univalent ions across the lamellae of swollen phospholipids. J. Mol. Biol. 1965, 13, 238-252.
15. MacDonald, R. C.; MacDonald, R. I.; Menco, B. Ph. M.; Takeshita, K; Subbarao, N. K.; Hu, L. Small-volume extrusion apparatus for preparation of large, unilamellar vesicles. Biochim. Biophys. Acta 1991, 1061, 297-303.
16. Wilchek, M.; Miron, T. Immobilization of enzymes and affinity ligands onto agarose via stable and uncharged carbamate linkages. Biochem. Int. 1982, 4, 629-635.
17. Beigi, F.; Yang, Q.; Lundahl, P. Immobilized-liposome chromatographic analysis of drug partitioning into lipid bilayers. J. Chromatogr. A 1995, 704, 315-321.
18. Bartlett, G. R. Phosphorus assay in column chromatography. J. Biol. Chem. 1959, 234, 466-468.
19. Kuboi, R.; Yano, K.; Komasawa, I. Evaluation of surface properties and partitioning of proteins in aqueous two-phase systems. Solvent Extr. Dev. Jpn. 1994, 1, 42-52.
20. Kuboi, R.; Yano, K.; Tanaka, H.; Komasawa, I. Evaluation of surface hydrophobicities during refolding process of carbonic anhydrase. J. Chem. Eng. Jpn. 1993, 26, 286-290.
21. Umakoshi, H.; Yoshimoto, M.; Shimanouchi, T.; Kuboi, R.; Komasawa, I. Model system for heat-induced translocation of cytoplasmic β-galactosidase across phospholipid bilayer membrane. Biotechnol. Prog. 1998, 14, 218-226.
22. Bradford, M. M. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle protein-dye binding. Anal. Biochem. 1976, 72, 248-254.
23. Jolles, P. Preparation and assay of enzymes. Methods Enzymol. 1962, 5, 12-13.
24. Creighton, T. E. Protein folding; W. H. Freeman and Company: New York, 1992; pp 301-351.
25. Roux, P.; Delepierre, M.; Goldberg, M. E.; Chaffotte, A.-F. Kinetics of secondary structure recovery during the refolding of reduced hen egg white lysozyme. J. Biol. Chem. 1997, 272, 24843-24849.
26. Maeda, Y.; Ueda, T.; Yamada, H.; Imoto, T.; The role of net charge on the renaturation of reduced lysozyme by the sulfhydryl-disulfide interchange reaction. Protein Eng. 1994, 7, 1249-1254.
27. Maeda, Y.; Yamada, H.; Ueda, T.; Imoto, T. Effect of additives on the renaturation of reduced lysozyme in the presence of 4 M urea. Protein Eng. 1996, 9, 461-465.
28. Ruoppolo, M.; Lundstrom-Ljung, J.; Talamo, F.; Pucci, P.; Marino, G. Effect of glutaredoxin and protein disulfide isomerase on the glutathione-dependent folding of ribonuclease A. Biochemistry 1997, 36, 12259-12267.
29. Rozema, D.; Gellman, S. H. Artificial chaperone-assisted refolding of denatured-reduced lysozyme: modulation of the competition between renaturation and aggregation. Biochemistry 1996, 35, 15760-15771.
30. Horwitz, J. α-Crystallin can function as a molecular chaperone. Proc. Natl. Acad. Sci. U.S.A. 1992, 89, 10449-10453.
31. Raman, B.; Ramakrishna, T.; Rao, Ch. M. Effect of chaperone-like alpha-crystallin on the refolding of lysozyme and ribonuclease A. FEBS Lett. 1997, 416, 369-372.
32. Cleland, J. L.; Hedgepeth, C.; Wang, D. I. C. Polyethylene glycol enhanced refolding of bovine carbonic anhydrase B. J. Biol. Chem. 1992, 267, 13327-13334.
33. Cleland, J. L.; Randolph, T. W. Mechanism of polyethylene glycol interaction with the molten globule folding intermediate of bovine carbonic anhydrase B. J. Biol. Chem. 1992, 267, 3147-3153.
34. Uversky, V. N.; Ptitsyn, O. B. Further evidence on the equilibrium "pre-molten globule state": four-state guanidinium chloride-induced unfolding of carbonic anhydrase B at low temperature. J. Mol. Biol. 1996, 255, 215-228.
35. Joseph, M.; Nagaraj, R. Unfolding of lysozyme by breaking its disulfide bridges results in exposure of hydrophobic sites. Biochem. Int. 1992, 26, 973-978.
36. Yamahara, K. Ota, H.; Kuboi, R. Characterization of stress responsive behaviors of proteins. J. Chem. Eng. Jpn. 1998, 31, 795-803.
37. Kuobi, R.; Yamahara, K.; Ota, H. Evaluation of denaturation and aggregate formation of enzyme under heat stress conditions. J. Chem. Eng. Jpn. 1997, 30, 1119-1122.
38. Hirose, M.; Yamashita, H. Partially folded state of the disulfide-reduced N terminal halfmolecule of ovotransferrin as a renaturation intermediate. J. Biol. Chem. 1991, 266, 14631-14638.
39. Katsumata, K.; Okazaki, A.; Kuwajima, K. Effect of GroEL on the re-folding kinetics of a-lactalbumin. J. Mol. Biol. 1996, 258, 827-838.
40. Matsubara, M.; Nohara, D.; Kurimoto, E.; Kuroda, Y.; Sakai, T. "Loose folding" and "delayed oxidation" procedures successfully applied for refolding of fully reduced hen egg white lysozyme. Chem. Pharm. Bull. 1993, 41, 1207-1210.
41. Xindu, G.; Chang, X. High-performance hydrophobic interaction chromatography as a tool for protein refolding. J. Chromatogr. 1992, 599, 185-194.
42. Altamirano, M. M.; Golbik, R.; Zahn, R.; Buckle, A. M.; Fersht, A. R. Refolding chromatography with immobilized mini-chaperones. Proc. Natl. Acad. Sci. U.S.A. 1997, 94, 3576-3578.
43. Batas, B.; Chaudhuri, J. B. Protein refolding at high concentration using size-exclusion chromatography. Biotechnol. Bioeng. 1996, 50, 16-23.
44. Maachupalli-Reddy, J.; Kelley, B. D.; Clark, E. De B. Effect of inclusion body contaminants on the oxidative renaturation of hen egg lysozyme. Biotechnol. Prog. 1997, 13, 144-150.
45. Umakoshi, H.; Shimanouchi, T.; Kuboi, R. Selective separation process of proteins based on the heat stress-induced translocation across phospholipid membranes. J. Chromatogr. B 1998, 711, 111-116.
46. Umakoshi, H.; Kuboi, R. Enzyme release from heat-stressed cell membranes as a function of hydrophobicity evaluated by using aqueous two-phase systems. J. Chromtogr. B 1998, 711, 217-222.
47. Umakoshi, H.; Kuboi, R.; Komasawa, I.; Tsuchido, T.; Matsumura, Y. Heat-induced translocation of cytoplasmic β-galactosidase across inner membrane of Escherichia coli. Biotechnol. Prog. 1998, 14, 210-217.