PURIFICATION AND CRYSTALS OF TYROSINE PHENOL-LYASE FROM ERWINIA-HERBICOLA

Authors
PLETNEV SV ISUPOV MN DAUTER Z WILSON KS FALEEV NG HARUTYUNYAN EG DEMIDKINA TV
Citation
Sv. Pletnev et al., PURIFICATION AND CRYSTALS OF TYROSINE PHENOL-LYASE FROM ERWINIA-HERBICOLA, Biochemistry and molecular biology international, 38(1), 1996, pp. 37-42
Citations number
18
Categorie Soggetti
Biology
Journal title
Biochemistry and molecular biology international → ACNP
ISSN journal
10399712
Volume
38
Issue
1
Year of publication
1996
Pages
37 - 42
Database
ISI
SICI code
1039-9712(1996)38:1<37:PACOTP>2.0.ZU;2-4
Abstract
New method of purification of tyrosine phenol-lyase from Erwinia herbi cola has been developed. The enzyme obtained is homogeneous and charac terised by a specific activity which is three times higher then that d escribed earlier. Crystals of holoenzyme complexed with monovalent cat ions have been grown from NaCl, KCl and (NH4)(2)SO4 containing solutio ns. The crystals belong to P6(2)22 space group. They are stable to the X-ray radiation and diffract up to 2.6-3.1 A. Asymmetric unit contain s one subunit of tetrameric molecule.