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 isome...

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Veröffentlicht in:	Connective tissue research 1985, Vol.14 (2), p.129-139
Hauptverfasser:	Iguchi, Hiroshi, Sano, Seiyo
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Oxidoreductases - metabolism Animals Bone and Bones - metabolism cadmium Cadmium - metabolism Cadmium - pharmacology Cadmium Poisoning - metabolism Chick Embryo chick embryos Copper - metabolism Humans In Vitro Techniques lysyl oxidase Protein-Lysine 6-Oxidase - antagonists & inhibitors Protein-Lysine 6-Oxidase - isolation & purification Protein-Lysine 6-Oxidase - metabolism zinc Zinc - metabolism Zinc - pharmacology
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