Purification of nitric oxide synthase from bovine brain: immunological characterization and tissue distribution.
作者信息
Ohshima H, Oguchi S, Adachi H, Iida S, Suzuki H, Sugimura T, Esumi H
机构信息
Biochemistry Division, National Cancer Center Research Institute, Tokyo, Japan.
出版信息
Biochem Biophys Res Commun. 1992 Feb 28;183(1):238-44. doi: 10.1016/0006-291x(92)91634-3.
Nitric oxide (NO) synthase (EC 1.14.23) was purified to homogeneity from bovine cerebrum. The molecular weight of NO synthase was estimated to be 150 kDa by both SDS/PAGE and gel filtration at high salt concentration. For activity, the enzyme required NADPH, Ca2+, calmodulin and tetrahydrobiopterin as cofactors. Rabbit polyclonal antibody to bovine brain NO synthase reacted with 150 kDa NO synthase in various bovine and rat organs, including the brain, pituitary and adrenal glands, but not with that in stimulated macrophages, indicating that there are at least two immunologically distinct NO synthases.
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