Purification and kinetic properties of a castor bean seed acid phosphatase containing sulfhydryl groups
作者： Paulo Afonso Granjeiro , Carmen Veríssima Ferreira , José Mauro Granjeiro , Eulázio Mikio Taga , Hiroshi Aoyama
DOI: 10.1034/J.1399-3054.1999.100201.X
关键词:
摘要: An acid phosphatase (EC 3.1.3.2) has been identified and purified from castor bean (Ricinus communis L., IAC-80) seed through sulphopropyl (SP)-Sephadex, diethylaminoethyl (DEAE)-Sephadex, Sephacryl S-200, Concanavalin A-Sepharose chromatography. The enzyme was 2000-fold to homogeneity, with a final specific activity of 3.8 μkat mg -1 protein. revealed single diffuse band on nondenaturing polyacrylamide gel electrophoresis, at pH 8.3. relative molecular mass, determined by high-performance liquid chromatography (HPLC), found be 60 kDa. had optimum 5.5 an apparent K m value for p-nitro-phenylphosphate 0.52 mM. enzyme-catalyzed reaction inhibited inorganic phosphate, fluoride, vanadate, molybdate, p-chloromercuribenzoate (pCMB), Cu 2+ Zn . strong inhibition pCMB, vanadate suggests the presence sulfhydryl groups essential catalysis. also recognized tyrosine-phosphate pyrophosphate (PP i ) as substrate. highest specificity constant (V max /K observed PP , making it potential physiological
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