Trapping of intermediates during the refolding of recombinant human epidermal growth factor (hEGF) by cyanylation, and subsequent structural elucidation by mass spectrometry

Protein Science

Volumn 7, Issue 4, 1998, Pages 1017-1028

  Wu, Jiang ^a,c   Yang, Ying ^a   Watson, J Throck ^a,b  

^a MICHIGAN STATE UNIVERSITY   (United States)

^b Michigan State University   (United States)

^c ABBOTT LABORATORIES   (United States)

Author keywords

1 cyano 4 dimethylamino pyridinium tetrafloroborate; Chemical cleavage; Disulfide structure; Folding intermediates; MALDI MS; Trapping

Indexed keywords

DISULFIDE; GAMMA UROGASTRONE; RECOMBINANT EPIDERMAL GROWTH FACTOR;

ARTICLE; DISULFIDE BOND; HUMAN; MASS SPECTROMETRY; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN ISOLATION; PROTEIN MODIFICATION; PROTEIN STRUCTURE;

EID: 0031954924     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560070419     Document Type: Article

References (30)

1. Balbach J, Forge V, van Nuland NAJ, Winder SL, Hore PJ, Dobson CM. 1995. Following protein folding in real time using NMR spectroscopy. Nature Struct Biol 2:865-870.
2. Chang JY. 1993. Identification of productive folding intermediates which account for the flow of protein folding pathway. J Biol Chem 268:4043-4049.
3. Chang JY, Schindler P, Ramseier U, Lai PH. 1995. The disulfide folding pathway of human epidermal growth factor. J Biol Chem 270(16):9207-9216.
4. Chang JY. 1996. The disulfide folding pathway of tick anticoagulant peptide (TAP), a Kunitz-type inhibitor structurally homologous to BPTI. Biochemistry 35:11702-11709.
5. Creighton TE. 1992. The disulfide folding pathway of BPTI. Science 256:111-114.
6. Creighton TE, Ewbank JJ. 1994. Disulfide-rearranged molten globule state of alpha-lactalbumin. Biochemistry 33:1534-1538.
7. Creighton TE, Goldenberg DP. 1984. Kinetic role of a meta-stable native-like two-disulphide species in the folding transition of bovine pancreatic trypsin inhibitor. J Mol Biol 179:497-526.
8. Darby NJ, Norin PE, Talbo G, Creighton TE. 1995. Refolding of bovine pancreatic trypsin inhibitor via non-native disulphide intermediates. J Mol Biol 249:463-477.
9. Frech C, Schmid FX. 1995. Influence of protein conformation on disulfide bond formation in the oxidative folding of rinonuclease T1. J Mol Biol 251:135-149.
10. Glocker MO, Arbogast B, Milley R, Cowgill C, Deinzer ML. 1994. Disulfide linkages in the in vitro refolded intermediates of recombinant human macrophage-colony-stimulating factor: Analysis of the sulfhydryl alkylation of free cysteine residues by fast-atom bombardment mass spectrometry. Proc Natl Acad Sci USA 91:5868-5872.
11. Goto Y, Hamaguchi K. 1981. Formation of the intrachain disulfide bond in the constant fragment of the immunoglobulin light chain. J Mol Biol 146:321-340.
12. Happersberger P, Cowgill C, Deinzer ML, Glocker MO. 1996. Proceedings of the 44th ASMS Conference on Mass Spectrometry and Allied Topics, Portland, OR: American Society for Mass Spectrometry. p 1050.
13. Hober S, Forsberg G, Palm G, Hartmanis M, Nilsson B. 1992. Disulfide exchange folding of insulin-like growth factor I. Biochemistry 31:1749-1756.
14. Jennings PA, Wright PE. 1993. Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin. Science 262:892-896.
15. Kim PS, Baldwin RL. 1990. Intermediates in the folding reactions of small proteins. Annu Rev Biochem 59:631-660.
16. Li YJ, Rothwarf DM, Scheraga HA. 1995. Mechanism of reductive protein unfolding. Nature Struct Biol 2:489-494.
17. Matthews CR. 1993. Pathways of protein folding. Annu Rev Biochem 62:653-683.
18. Ptitsyn OB. 1995. Structures of folding intermediates. Curr Opin Struct Biol 5:74-78.
19. Rothwarf DM, Scheraga HA. 1991. Regeneration and reduction of native bovine pancreatic ribonuclease A with oxidized and reduced dithiothreitol. J Am Chem Soc 113:6293-6294.
20. Rothwarf DM, Scheraga HA. 1993a. Regeneration of bovine pancreatic ribonuclease A. 1. Steady-state distribution. Biochemistry 32:2671-2679.
21. Rothwarf DM, Scheraga HA. 1993b. Regeneration of bovine pancreatic ribonuclease A. 2. Kinetics of regeneration. Biochemistry 32:2680-2689.
22. Rothwarf DM, Scheraga HA. 1993c. Regeneration of bovine pancreatic ribonuclease A. 3. Dependence on the nature of the redox reagent. Biochemistry 32:2690-2697.
23. Rothwarf DM, Scheraga HA. 1993d. Regeneration of bovine pancreatic ribonuclease A. 4. Temperature dependence of the regeneration rate. Biochemistry 32:2698-2703.
24. Smith DL, Zhou ZR. 1990. Strategies for locating disulfide bonds in proteins. Methods Enzymol 193:374-389.
25. Torella C, Ruoppolo M, Marino G, Pucci P. 1994. Analysis of RNase A refolding intermediates by electrospray/mass spectrometry. FEBS Letters 352:301-306.
26. Weissman JS, Kim PS. 1991. Reexamination of the folding of BPTI: Predominance of native intermediates. Science 253:1386-1393.
27. Weissman JS, Kim PS. 1992a. Kinetic role of nonnative species in the folding of bovine pancreatic trypsin inhibitor. Proc Natl Acad Sci USA 89:9900-9904.
28. Weissman JS, Kim PS. 1992b. The pro region of BPTI facilitates folding. Cell 71:841-851.
29. Wu J, Watson JT. 1997. A novel methodology for assignment of disulfide bond pairings in proteins. Protein Sci 6:391-398.
30. Xu X, Rothwarf DM, Scheraga HA. 1996. Nonrandom distribution of the one-disulfide intermediates in the regeneration of ribonuclease A. Biochemistry 35:6406-6417.