Purification of Penicillin Amidohydrolase, an Enzyme for Semisynthetic Procedures
| Autor: | Jiří Jiráček, Tomislav Barth, Ivan Svoboda, Jiří Velek, Ivo Bláha, Jan Pospíšek |
|---|---|
| Rok vydání: | 1992 |
| Předmět: |
chemistry.chemical_classification
Chromatography biology Chemistry Peptide General Chemistry Penicillin amidase Exopeptidase medicine.disease_cause Trypsin chemistry.chemical_compound Enzyme Affinity chromatography Biochemistry medicine Peptide synthesis biology.protein Escherichia coli medicine.drug |
| Zdroj: | Collection of Czechoslovak Chemical Communications. 57:2187-2191 |
| ISSN: | 1212-6950 0010-0765 |
| DOI: | 10.1135/cccc19922187 |
| Popis: | Penicillin amidohydrolase (EC 3.5.1.11.) is one of the few enzymes used successfully for deprotection of primary amino groups of semisynthetic peptides. The available material is usually contamined by endo- and exopeptidases. We managed to prepare the enzyme devoid of trypsin- and chymotrypsin-like activities using affinity chromatography with specific ligands: Gly-D-Phe-Phe-Tyr-Thr-Pro-Lys-Thr (the fF peptide) and Leu-Gly-Val-D-Arg-Arg-Gly-Phe (the rR peptide). For further purification of the enzyme affinity chromatography with N-phenylacetyl-D-tert-Leu as a ligand was used. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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