Literature DB >> 2338148

Purification and partial characterization of rat liver soluble catechol-O-methyltransferase.

C Tilgmann1, N Kalkkinen.   

Abstract

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.

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Year:  1990        PMID: 2338148     DOI: 10.1016/0014-5793(90)80774-d

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  3 in total

1.  PLS modelling of structure-activity relationships of catechol O-methyltransferase inhibitors.

Authors:  T Lotta; J Taskinen; R Bäckström; E Nissinen
Journal:  J Comput Aided Mol Des       Date:  1992-06       Impact factor: 3.686

2.  Clinical Potential of Catechol-OMethyltransferase (COMT) Inhibitors as Adjuvants in Parkinson's Disease.

Authors:  P T Ménnistó
Journal:  CNS Drugs       Date:  1994-03       Impact factor: 5.749

3.  Production of rat soluble and membrane-bound catechol O-methyltransferase forms from bifunctional mRNAs.

Authors:  J Tenhunen; I Ulmanen
Journal:  Biochem J       Date:  1993-12-15       Impact factor: 3.857

  3 in total

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