-transparent.png){kind=logo}
It has been reported that bovine aorta amine oxidase oxidizes lysine residues in tropoelastin to allysine (Rucker, R.B. and O'Dell, B.L. (1971) Biochim. Biophys. Acta 235, 32-43). Pure bovine aorta amine oxidase was isolate by DEAE-cellulose, hydroxylapatite, Bio-Gel A-1.5 m and concanavalin A-Sepharose 4B chromatography. Enzymatic, chromatographic and immunochemical tests disclosed that pure bovine aorta amine oxidase was not a lysyl oxidase capable of oxidizing the lysine residues of tropoelastin to allysine; The bovine aorta amine oxidase preparation used by Rucker and O'Dell appears to have been contaminated with lysyl oxidase which is the emzyme that oxidizes some of the lysine residues in tropoelastin and tropocollagen to allysine.
J J Shieh, and
R Tamaye, and
K T Yasunobu
April 1971,
Biochimica et biophysica acta,
J J Shieh, and
R Tamaye, and
K T Yasunobu
April 1974,
Biochimica et biophysica acta,
J J Shieh, and
R Tamaye, and
K T Yasunobu
January 1979,
The Biochemical journal,
J J Shieh, and
R Tamaye, and
K T Yasunobu
January 1976,
Archives of oral biology,
J J Shieh, and
R Tamaye, and
K T Yasunobu
October 1992,
Protein expression and purification,
J J Shieh, and
R Tamaye, and
K T Yasunobu
February 1983,
Life sciences,
J J Shieh, and
R Tamaye, and
K T Yasunobu
December 2018,
Biochemistry,
J J Shieh, and
R Tamaye, and
K T Yasunobu
January 1986,
Connective tissue research,
J J Shieh, and
R Tamaye, and
K T Yasunobu
September 1982,
Analytical biochemistry,
J J Shieh, and
R Tamaye, and
K T Yasunobu
January 1983,
Methods in enzymology,
