Cadmium- or Zinc-Binding to Bone Lysyl Oxidase and Copper Replacement

Lysyl oxidase was purified to about 3,000- to 5,000-fold from epiphyseal cartilages of chick embryos. Purification was accomplished by sequential column chromatographies of collagen-sepharose, DEAE-Cellulose and Sephacryl S-200. The molecular weight of the most purified enzyme from 4 different isomers as determined by gel-filtration technique using Sephacryl S-200 column was 32,000 and the purified enzyme contained one copper atom per mole.