Evidence for peptide synthesis in the course of in vitro proteolysis
1997
Lorenzen, P.Chr. | Goepfert, A. | Schieber, A. | Brueckner, H.
The present paper reports on studies concerned with furnishing evidence for peptide synthesis in the course of in vitro proteolysis. To this end, the oxidized chain B from insulin (INS) was subjected to tryptic proteolysis. HPLC -as well as amino acid - and sequence analytical studies have shown that the heptapeptide INS 23-29 liberated by way of hydrolysis is linked by tryptic synthesis via transpeptidation or condensation to form a dimer which accounts for 15 % of the amount of monomer. The results of the model trials show clearly that during in vitro proteolysis chemical reactions beyond hydrolytic cleavage of peptide bonds take place. In principle, plastein-like reactions (transpeptidation, condensation) can occur during each in vitro proteolysis.
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