Purification of Penicillin Amidohydrolase, an Enzyme for Semisynthetic Procedures

descriptionPublicationkeyboard_double_arrow_right Article 01 Jan 1992 English Publisher:Institute of Organic Chemistry & BiochemistryJournal:Collection of Czechoslovak Chemical Communications, volume 57, pages 2,187-2,191 (issn: 0010-0765, eissn: 1212-6950,

Authors: Ivo Bláha; Ivan Svoboda; Tomislav Barth; Jiří Jiráček; Jiří Velek; Jan Pospíšek;

doi: 10.1135/cccc19922187

Purification of Penicillin Amidohydrolase, an Enzyme for Semisynthetic Procedures

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Abstract

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.

Related Organizations

Czechoslovak Academy of Sciences
Czech Republic
Czech Academy of Sciences
Czech Republic

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