A purification procedure for the isolation of homogeneous preparations of bovine aorta amine oxidase and a study of its lysyl oxidase activity.
Biochim Biophys Acta, 1975/2/19;377(2):229-38.
Shieh JJ, Tamaye R, Yasunobu KT
PMID: 235299
Abstract
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.
MeSH terms
Amino Acid Oxidoreductases; Animals; Aorta; Cattle; Chromatography; Chromatography, Affinity; Chromatography, Gel; Elastin; Electrophoresis, Disc; Kinetics; Molecular Weight; Protein-Lysine 6-Oxidase; Structure-Activity Relationship
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