来自普通脱硫弧菌的两种具有无机焦磷酸酶活性的蛋白质的纯化与表征：红素氧还蛋白和一种新的高活性酶。
Purification and characterization of two proteins with inorganic pyrophosphatase activity from Desulfovibrio vulgaris: rubrerythrin and a new, highly active, enzyme.
作者信息
Liu M Y, Le Gall J
机构信息
Department of Biochemistry, School of Chemical Sciences, University of Georgia, Athens 30602.
出版信息
Biochem Biophys Res Commun. 1990 Aug 31;171(1):313-8. doi: 10.1016/0006-291x(90)91394-8.
The inorganic pyrophosphatase activity of a soluble extract from the strict anaerobe, sulfate-reducing, Desulfovibrio vulgaris, is readily resolved into two peaks. After purification, two active proteins with very dissimilar properties are obtained. One is the non-heme iron-containing rubrerythrin, with a specific activity of 350 pyrophosphate hydrolyzed, min-1, mg protein-1. The other, a protein of Mr = 39,000, with a specific activity of 12,000.
严格厌氧的硫酸盐还原菌——普通脱硫弧菌的可溶性提取物中的无机焦磷酸酶活性很容易分离成两个峰。纯化后，得到了两种性质差异很大的活性蛋白。一种是不含血红素的含铁红素蛋白，比活性为每分钟每毫克蛋白质水解350个焦磷酸。另一种是分子量为39000的蛋白质，比活性为12000。
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