Open AccessPurification and Studies of Catechol‐ O ‐Methyltransferase of Rat Liver
Author(s) -
Assicot Marcel,
Bohuon Claude
Publication year - 1970
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1970.tb00877.x
Subject(s) - size exclusion chromatography , dithiothreitol , chemistry , ultracentrifuge , chromatography , catechol , enzyme , incubation , fractionation , reagent , salt (chemistry) , homogeneous , filtration (mathematics) , sedimentation equilibrium , biochemistry , organic chemistry , physics , statistics , mathematics , thermodynamics
Rat liver catechol‐ O ‐methyltransferase was purified approximately 450‐fold by salt fractionation, get filtration, hydroxyapatite treatment, and ion‐exchange chromatography. The final enzyme preparation is homogeneous when subjected to disc electrophoresis and sedimentation analysis in the ultracentrifuge. The purified enzyme is very labile; reversible inactivation occurs upon storage. Reactivation is obtained by incubation with dithiothreitol. The molecular weight, determined by gel filtration, is 24000.