Abstract:
:We have recently developed a method to produce native human proinsulin using a bacterial expression system. A proinsulin fusion protein was recovered from inclusion bodies and cleaved using cyanogen bromide. The released proinsulin polypeptide was S-sulfonated and purified by anion exchange chromatography. Following refolding, proinsulin was purified by reversed-phase high-performance liquid chromatography. Combined peptide mapping and mass spectrometric analysis indicated that the proinsulin contained the correct disulfide bridging pattern. This proinsulin will be used to study the specificity of the furin/PC family of converting enzymes by using it as a substrate in a recently developed assay.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Cowley DJ,Mackin RBdoi
10.1016/s0014-5793(96)01511-6subject
Has Abstractpub_date
1997-02-03 00:00:00pages
124-30issue
2-3eissn
0014-5793issn
1873-3468pii
S0014-5793(96)01511-6journal_volume
402pub_type
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