The complete primary structure of chick lysyl oxidase was determined by recombinant DNA techniques. The nucleotide sequence of contiguous chick lysyl oxidase cDNA clones contained an open reading frame of 1260 bases which encodes a predicted protein of 420 amino acid residues (48,150 Da). In comparison to the deduced primary structure of rat lysyl oxidase, the chick enzyme is larger in size and exhibits a strong conservation of sequence within the latter two thirds of the molecule (92% identity) and a high degree of divergence in the first 150 amino acid residues (60% identity allowing for several insertions in both sequences). The developmental steady-state levels of lysyl oxidase mRNA together with the mRNAs encoding two of the enzyme's substrates (tropoelastin and type I collagen) increased between 8 and 16 days of embryonic development. Although levels of lysyl oxidase mRNA increased during aortic embryogenesis, the specific activity of the enzyme remained fairly constant suggesting that lysyl oxidase activity increases in direct proportion to total protein synthesis and cell number. In situ hybridization showed that the spatial expressions of lysyl oxidase and tropoelastin transcripts differ suggesting that the enzyme and substrate genes are differentially regulated within the cells of the arterial wall.