Original title: Desoctapeptideinsulin fragments formed by chymotryptic cleavage and suitable for modification of insulin in positions A 14 and B 16
Authors: Koubová, V. ; Barthová, J. ; Kašička, Václav ; Ubik, Karel ; Barth, Tomislav ; Bezouška, K.
Document type: Papers
Conference/Event: Biologically Active Peptides. Conference /6./, Praha (CZ), 1999-04-21 / 1999-04-23
Year: 1999
Language: eng
Abstract: The molecule of desoctapeptide insulin is cleaved by ŕ-chymotrypsin at the three tyrosine residues. The fragments with tyrosine C-terminal residues are candidates of semisynthetic modification. They were isolated and characterized by HPLC, capillary electrophoresis and mass spectrometry.
Keywords: DOI-Fragments
Project no.: CEZ:AV0Z4055905 (CEP), PZ-Z2/32 (CEP)
Funding provider: GA MPO
Host item entry: Biologically Active Peptides

Institution: Institute of Organic Chemistry and Biochemistry AS ČR (web)
Document availability information: Fulltext is available at the institute of the Academy of Sciences.
Original record: http://hdl.handle.net/11104/0089384

Permalink: http://www.nusl.cz/ntk/nusl-28300


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Research > Institutes ASCR > Institute of Organic Chemistry and Biochemistry
Conference materials > Papers