Abstract:
:Nerve growth factor (NGF) is a member of the neurotrophin family. These growth factors support neuronal survival and differentiation. Neurotrophins are synthesized as pre-pro-proteins. Whereas the pre-sequences mediate secretion, the function of the pro-peptides is largely unknown. To test the role of the pro-sequence as a folding enhancer, recombinant human pro-NGF (rh-pro-NGF) was produced in Escherichia coli. The oxidative refolding of rh-pro-NGF and rh-NGF was studied using electrospray mass spectrometry (ESIMS) time-course analysis. This analysis permitted both the identification and quantification of intermediates present during the process. The disulfide bonds formed at different times of the refolding processes were characterized by proteolytic digestion followed by matrix assisted laser desorption ionization mass spectrometry (MALDIMS) analysis. Folding yields and kinetics of rh-pro-NGF were significantly enhanced when compared to the in vitro refolding of mature rh-NGF. These results suggest that the pro-sequence of NGF promotes folding of the mature part.
journal_name
J Mol Bioljournal_title
Journal of molecular biologyauthors
Rattenholl A,Ruoppolo M,Flagiello A,Monti M,Vinci F,Marino G,Lilie H,Schwarz E,Rudolph Rdoi
10.1006/jmbi.2000.4295keywords:
subject
Has Abstractpub_date
2001-01-19 00:00:00pages
523-33issue
3eissn
0022-2836issn
1089-8638pii
S0022-2836(00)94295-5journal_volume
305pub_type
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