Studies on lysyl oxidase of bovine ligamentum nuchae and bovine aorta.
Lysyl oxidase had been purified to near homogeneity from bovine aorta and bovine ligamentum nuchae employing a modification of methods described by Harris et al., and Stassen and his colleagues. The aortic enzyme gives rise to at least three peaks and the ligament enzyme resolves into at least four peaks upon chromatography on DEAE cellulose. The molecular weight of each peak of both enzymes is approximately 30,000 daltons in sodium dodecyl sulfate. The aortic enzyme aggregates to species with molecular weights varying from approximately 60,000 to 1,000,000 daltons upon dialysis out of urea into phosphate-buffered saline. Temperature studies reveal that lysyl oxidase is stable to temperatures as high as 80 degrees C, although the assay optimum is 52 degrees C. Studies in progress suggest the temperature dependency of assay may reflect conformational changes in the elastin substrate.
D000594:Amino Acid Oxidoreductases / Q000302:isolation & purification*; D000818:Animals; D001011:Aorta / Q000201:enzymology*; D002417:Cattle; D002846:Chromatography, Affinity; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D004589:Electrophoresis, Disc; D008022:Ligaments / Q000201:enzymology*; D008970:Molecular Weight; D009333:Neck; D008249:Protein-Lysine 6-Oxidase / Q000302:isolation & purification*; D013696:Temperature
D000594:Amino Acid Oxidoreductases; D008249:Protein-Lysine 6-Oxidase