The quails, Coturnix coturnix japonica, were fed with saline of CdCl2 or mixture of CdCl2 and PbCl2 orally, and were sacrificed after 16 days. The cadmium binding metallothionein was purified from the quail liver by the Sephedax G-75 permeation chromatography and centrifugal devices for concentration. After that the protein was tested by UV spectrophotometer and analysis of amino acid composition. The results demonstrate that the quail metallothionein contains 63 amino acid residuals, which has the general biochemical properties of mammal metallothionein: spectroscopic feathers typical of cadmium thiolate clusters, low molecular weight (6 614 Da), high metal (cadmium) content and the high level of cysteine content (about 31.82%). The cadmium-hemoglobin saturation assay was applied for quantification of metallothionein in the quail liver, the results showed that the synthesis of metallothionein in the quail liver can be induced by heavy metal cadmium and lead, and the amount of the liver metallothionein was increased with the heavy metal concentration exposed. The induction of metallothionein in the quail liver suggests that the heavy metal homeostasis mechanism in quails may have evolved similarly to mammals.