Purification and characterization of acid phosphatase from yellow lupin (Lupinus luteus) seeds

被引:44
作者
Olczak, M
Watorek, W
Morawiecka, B
机构
[1] Inst. of Biochem. and Molec. Biology, Wrocław University, 50-137 Wrocław
来源
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY | 1997年 / 1341卷 / 01期
关键词
acid phosphatase; lupin; seed; purification;
D O I
10.1016/S0167-4838(97)00055-1
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Acid phosphatase (EC 3.1.3.2) from yellow lupin (Lupinus luteus) seeds was purified to homogeneity by ammonium sulphate fractionation, affinity chromatography, cation-exchange chromatography, gel filtration or reverse-phase HPLC. The enzyme is a dimer with the 50 kD and 44 kD subunits and contains 7.3% of carbohydrate, forming at least four oligosaccharide chains, The optimum pH for the enzyme is 5.4. The apparent K-m for p-nitrophenyl phosphate was estimated to be 0.28 mM and V-max = 1780 IU/mg of protein, The purified phosphatase has the highest specific activities reported for any plant acid phosphatases measured for any native or synthetic substrate, The enzyme has broad specificity; however, cyclic nucleotides, pyrophosphate or phytate are not cleaved. It is inhibited by molybdate, fluoride and phosphate. There is no change in the enzyme activity in the presence of EDTA, phenanthroline and tartrate. (C) 1997 Elsevier Science B.V.
引用
收藏
页码:14 / 25
页数:12
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