Purification and properties of calf liver γ-butyrobetaine hydroxylase

Atsushi Kondo, John S. Blanchard, Sasha Englard

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30 Scopus citations

Abstract

Calf liver γ-butyrobetaine hydroxylase has been purified some 400-fold by DEAE, gel permeation, and hydroxylapatite chromatography. The homogeneous enzyme is a dimer of 46,000-dalton subunits. The Km values for substrates and cofactors and the apparent activation constants for ascorbate and catalase have been determined. Inhibition of the enzyme by a number of divalent metals supports the function of sulfhydryl groups in metal binding. An antibody to the enzyme has been obtained; this does not cross-react with homogeneous γ-butyrobetaine hydroxylase from a Pseudomonas strain. The antibody, coupled to Sepharose 4B, has been used to purify the calf liver hydroxylase 350-fold in one step.

Original languageEnglish (US)
Pages (from-to)338-346
Number of pages9
JournalArchives of Biochemistry and Biophysics
Volume212
Issue number2
DOIs
Publication statusPublished - Dec 1981

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ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology

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