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Lysyl hydroxylase (peptidyllysine, 2-oxoglutarate: oxygen 5-oxidoreductase, EC 1.14.11.4) has a high affinity for columns of concanavalin A-agarose, which was markedly reduced in the presence of alpha-methyl-D-mannoside, suggesting that the enzyme is a glycoprotein. Once bound, the enzyme could not be eluted with the glycoside alone, whereas an effective elution was achieved by a combination of alpha-methyl-D-mannoside and ethylene glycol. The data thus suggest that hydrophobic interaction stabilized the complex of the enzyme with the column. This information was applied to obtain a lysyl hydroxylase purification of about 3000-fold with a recovery of more than 10% from extract of chick embryos by relatively simple steps.
T M Turpeenniemi, and
U Puistola, and
H Anttinen, and
K I Kivirikko
July 1981,
Journal of neurochemistry,
T M Turpeenniemi, and
U Puistola, and
H Anttinen, and
K I Kivirikko
February 1979,
Biotechnology and bioengineering,
T M Turpeenniemi, and
U Puistola, and
H Anttinen, and
K I Kivirikko
January 1975,
Acta biologica et medica Germanica,
T M Turpeenniemi, and
U Puistola, and
H Anttinen, and
K I Kivirikko
May 1976,
Analytical biochemistry,
T M Turpeenniemi, and
U Puistola, and
H Anttinen, and
K I Kivirikko
May 1985,
Journal of biochemistry,
T M Turpeenniemi, and
U Puistola, and
H Anttinen, and
K I Kivirikko
August 1973,
Biochimica et biophysica acta,
T M Turpeenniemi, and
U Puistola, and
H Anttinen, and
K I Kivirikko
November 1978,
Biochimica et biophysica acta,
T M Turpeenniemi, and
U Puistola, and
H Anttinen, and
K I Kivirikko
December 1979,
Biochemistry,
T M Turpeenniemi, and
U Puistola, and
H Anttinen, and
K I Kivirikko
June 2006,
CSH protocols,
T M Turpeenniemi, and
U Puistola, and
H Anttinen, and
K I Kivirikko
January 1981,
Methods in enzymology,
