Purification and partial characterization of rat liver soluble catechol‐ O‐methyltransferase

FEBS Letters

Kalkkinen, Nisse²  Tilgmann, Carola¹ 

[1] Orion Corporation, Genetic Engineering Laboratory, Valimotie 7,00380 Helsinki, Finland;Institute of Biotechnology, University of Helsinki, Karvaamokuja 3,00380 Helsinki, Finland

关键词: Methylating enzyme;    Catechol-O-methyltransferase;    soluble;    S-COMT;    soluble catechol-O-methyltransferase;    SDS-PAGE;    sodium dodecylsulfate;    RP;    reversed phase;    HPLC;    high performance liquid chromatography;    TFA;    trifluoroacetic acid;   

DOI  :  10.1016/0014-5793(90)80774-D

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown