Comparison of lysyl oxidase from bovine lung and aorta.
A prior report had concluded that bovine lung lysyl oxidase displayed an unusual resistance to inhibition by beta-aminopropionitrile (BAPN) in contrast to the enzyme isolated from other connective tissues. Therefore, lysyl oxidase was purified from fetal bovine lung and from aorta of young calves by parallel procedures, and key chromatographic and catalytic properties of these enzymes were directly compared. The enzymes prepared from both tissues each demonstrated the same multiplicity of enzyme species which resolve on DEAE-cellulose and otherwise demonstrated the same chromatographic behavior on gel exclusion media and on collagen-Sepharose and Cibacron blue-Sepharose columns. The activities of the unresolved but partially purified enzyme species of lung and of aortic lysyl oxidase were each fully inhibitable by approximately the same low (mu molar) concentrations of BAPN. Thus, the enzymes of both tissues were found to be very similar to each other by several criteria.
D000594:Amino Acid Oxidoreductases / Q000378:metabolism*; D000818:Animals; D001011:Aorta / Q000201:enzymology*; D002417:Cattle; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D007700:Kinetics; D008168:Lung / Q000201:enzymology*; D008970:Molecular Weight; D009928:Organ Specificity; D008249:Protein-Lysine 6-Oxidase / Q000302:isolation & purification / Q000378:metabolism*
D000594:Amino Acid Oxidoreductases; D008249:Protein-Lysine 6-Oxidase