Abstract
Summary
Evidence is presented which demonstrates that chick bone contains an amine oxidase which could function in the oxidative deamination of collagen lysyl residues to α-amino adipic acid-Δ-semialdehyde residues. This function would be directly related to the process of collagen cross-linking. The enzyme was slightly soluble, had an apparent molecular weight from gel filtration studies of 250,000, and could be partially purified by ammonium sulfate precipitation. When benzylamine was used as the substrate in kinetic studies, a K mapp of 0.15 mM was obtained. The enzyme required copper and pyridoxal phosphate and was competitively inhibited by beta-amino propionitrile, butylamine, and the peptide, lysine-vasopressin. Benzylamine oxidation was noncompetively inhibited by ascorbic acid, penicillamine, and isoniazid. The lysine in lysine-vasopressin was oxidized to the semial-dehyde. The pH optimum for oxidations was approximately pH 7.7.
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