Tilgmann C, Kalkkinen N
Orion Corporation, Genetic Engineering Laboratory, Helsinki, Finland.
FEBS Lett. 1990 May 7;264(1):95-9. doi: 10.1016/0014-5793(90)80774-d.
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.