Abstract：
:To investigate the contribution of the N-terminal sequence of h-EGF to its biological activity and the formation of three intramolecular disulfide bonds by oxidative refolding via air oxidation, five derivatives of h-EGF with a single N-terminal amino acid deletion were synthesized by solid-phase synthesis. The homogeneity of the synthetic peptides was confirmed by analytical reversed-phase HPLC, amino acid analysis, and FAB-MS. The pairing of the three disulfide bridges in synthetic peptides was determined by thermolytic digestion. All N-truncated derivatives of h-FGF formed the correct intramolecular three disulfide linkages during oxidative refolding and had equipotent activity in both EGF receptor binding on A-431 epidermoid carcinoma cells and mitogenesis on NIH-3T3 fibroblast cells, compared with authentic h-EGF. The results suggested that the five residues from N-terminal sequence of h-EGF have no effect on the formation of the correct disulfide linkages in h-EGF and do not exert a significant influence on its biological activity.
journal_name
Peptidesjournal_title
Peptidesauthors
Shin SY,Shimizu M,Ohtaki T,Munekata Edoi
10.1016/0196-9781(94)00181-2subject
Has Abstractpub_date
1995-01-01 00:00:00pages
205-10issue
2eissn
0196-9781issn
1873-5169pii
0196-9781(94)00181-2journal_volume
16pub_type
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