TY - JOUR
T1 - Purification and properties of calf liver γ-butyrobetaine hydroxylase
AU - Kondo, Atsushi
AU - Blanchard, John S.
AU - Englard, Sasha
N1 - Funding Information:
1 This work was supported by Grant Dr. Sasha Englard, and GM-07452 Blanchard from the National Institutes ‘To whom reprint requests should
PY - 1981/12
Y1 - 1981/12
N2 - 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.
AB - 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.
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U2 - 10.1016/0003-9861(81)90374-X
DO - 10.1016/0003-9861(81)90374-X
M3 - Article
C2 - 6798936
AN - SCOPUS:0019765462
SN - 0003-9861
VL - 212
SP - 338
EP - 346
JO - Archives of Biochemistry and Biophysics
JF - Archives of Biochemistry and Biophysics
IS - 2
ER -