ABSTRACT
The discovery of lysyl oxidase prompted a great interest in this enzyme and many attempts were made to purify it. Initially, in order to show its possible lysyl oxidase activity, there was considerable interest in determining whether or not Serum amine oxidase was active in the production of cross-links in collagen and elastin. Difficulties in releasing lysyl oxidase from its substrates may be indicative of the fact that a large fraction of this enzyme is not free but linked to collagen or elastin. It might be useful to treat preparations with proteases before purification. Lysyl oxidase acts on collagen and elastin. Lysyl oxidase can act upon lysine-containing synthetic peptides. Lysyl oxidase has been shown to be a cupric-copper protein. Fibroblasts and smooth muscle cells secrete measurable amounts of lysyl oxidase into the culture medium, a finding that is consistent with the hypothesis of an extracellular site for aldehyde formation.
