摘要
通过DEAE－纤维素层析，羟基磷灰石层析及Sepharose CL-6B层析，从猪脾中获得了纯的血红素加氧酶。纯化的酶在聚丙烯酰胺凝胶电泳及SDS－聚丙烯酰胺电泳中均呈现单一条带。测得该酶分子量约为30500道尔顿，含272个氨基酸残基。氨基酸组成分析表明该酶中谷氨酸、谷氨酰胺含量丰富，而半胱氨酸和色氨酸含量低。在280nm处具有较低的消光系数（E1cm^1%=8.12)，而在406nm处具有强烈的光吸收。Triton×-100和EDTA对酶有稳定作用。
A Heme oxygenase from poricne spleen has been purified to homogeneity by DEAE-cellulose chromatography^ hydroxyapatite chromatography and sepharose CL-6B Chromatography. The purified enzyme showed a single protein band on polyacrylamide electrophoresis and SDS-polyacrylamide electroporesis with a molecular weight of 30500. The enzyme consists of about 272 amino acid residues. Amino acid analysis of the purified enzyme revealed an abundance of glutamine and glutarriic acid residues, a low tryptophan content, et had a relatively low extinction coefficient at 280 (E%11cm = 3. 12) and had an intense absorption at 406nm. The enzyme are stable in a medium containing triton X-100 and EDTA.
