Monomeric B27 Lys destripeptide insulin: semisynthesis, characterization and biological activity

In this paper, we report the semisynthesis of B27 Lys destripeptide insulin (B27 Lys DTrI), i.e. destetrapeptide insulin with an additional Lys residue at the C-terminus of B-chain. B27 Lys DTrI is also monomeric as shown by gel filtration. Its in vivo biological activity is 80% in comparison with t...

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Bibliographic Details
Published inSheng wu hua hsüeh yü sheng wu wu li hsüeh pao Vol. 35; no. 3; p. 215
Main Authors Ding, Jin-Guo, Cui, Da-Fu, Zhang, You-Shang
Format Journal Article
LanguageEnglish
Published China 01.03.2003
Subjects
Amino Acid Sequence
Animals
Binding, Competitive
Blood Glucose - drug effects
Blood Glucose - metabolism
Chromatography, High Pressure Liquid
Chromatography, Thin Layer
Electrophoresis, Polyacrylamide Gel
Humans
Hypoglycemic Agents - chemical synthesis
Hypoglycemic Agents - isolation & purification
Hypoglycemic Agents - pharmacology
Insulin - analogs & derivatives
Insulin - chemical synthesis
Insulin - isolation & purification
Insulin - pharmacology
Mice
Peptide Fragments - chemistry
Peptide Fragments - metabolism
Peptide Fragments - pharmacology
Receptor, Insulin - metabolism
Swine
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Summary:In this paper, we report the semisynthesis of B27 Lys destripeptide insulin (B27 Lys DTrI), i.e. destetrapeptide insulin with an additional Lys residue at the C-terminus of B-chain. B27 Lys DTrI is also monomeric as shown by gel filtration. Its in vivo biological activity is 80% in comparison with that of native insulin. The addition of a Lys residue at the C-terminus of B-chain makes it possible to obtain monomeric B27 Lys DTrI from a precursor expressed in Saccharomyces cerevesiae by tryptic hydrolysis instead of the less efficient tryptic transpeptidation.
ISSN:0582-9879