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Purification and partial characterization of rat liver soluble catechol‐ O ‐methyltransferase
Author(s) -
Tilgmann Carola,
Kalkkinen Nisse
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80774-d
Subject(s) - catechol , chemistry , molecular mass , catechol o methyl transferase , enzyme , methyltransferase , high performance liquid chromatography , chromatography , biochemistry , intramolecular force , affinity chromatography , stereochemistry , methylation , allele , gene
The rat liver soluble catechol‐ O ‐methyltransferase (EC 2.1.1.6.) has been purified utilizing a combination of conventional chromatography and HPLC. The purified enzyme has a molecular mass of 25 kDa, a pI of 5.1, and exists in two forms which differ in the nature of their intramolecular disulfide bonds. This difference causes these two protein forms to behave differently in reversed phase chromatography.