Purification and properties of calf liver γ-butyrobetaine hydroxylase

Atsushi Kondo, John S. Blanchard, Sasha Englard

Research output: Contribution to journalArticle

30 Citations (Scopus)

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
StatePublished - 1981

Fingerprint

gamma-Butyrobetaine Dioxygenase
Liver
Purification
Enzymes
Metals
Antibodies
Durapatite
Mixed Function Oxygenases
Chromatography
Pseudomonas
Permeation
Dimers
Catalase
Sepharose
Gel Chromatography
Gels
Chemical activation
Substrates

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Purification and properties of calf liver γ-butyrobetaine hydroxylase. / Kondo, Atsushi; Blanchard, John S.; Englard, Sasha.

In: Archives of Biochemistry and Biophysics, Vol. 212, No. 2, 1981, p. 338-346.

Research output: Contribution to journalArticle

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