Tissot G, Job D, Douce R, Alban C
Unité Mixte, CNRS/Rhône-Poulenc (UMR 41), Rhone-Poulenc Agrochimie, Lyon, France.
Biochem J. 1996 Mar 1;314 ( Pt 2)(Pt 2):391-5. doi: 10.1042/bj3140391.
Biotin holocarboxylase synthetase was partially purified from pea leaves by a sequence of ammonium sulphate fractionation and DEAE 52-cellulose chromatography. Enzyme activity was assayed using apo-(biotin carboxyl carrier protein) from an Escherichia coli bir A mutant affected in biotin holocarboxylase synthetase activity. Conditions for optimal catalytic activity and biochemical parameters of the plant enzyme were determined. This is the first direct evidence of the existence of biotin holocarboxylase synthetase activity in plants.
通过一系列硫酸铵分级分离和DEAE 52 - 纤维素色谱法从豌豆叶中部分纯化了生物素全羧化酶合成酶。使用来自受生物素全羧化酶合成酶活性影响的大肠杆菌bir A突变体的脱辅基(生物素羧基载体蛋白)测定酶活性。确定了植物酶的最佳催化活性条件和生化参数。这是植物中存在生物素全羧化酶合成酶活性的首个直接证据。