Kuciel R, Bakalova A, Mazurkiewicz A, Bilska A, Ostrowski W
Institute of Medical Biochemistry, N. Copernicus Academy of Medicine, Kraków, Poland.
Biochem Int. 1990 Oct;22(2):329-34.
Prostatic acid phosphatase [E.C. 3.1.3.2.] is a dimeric protein consisting of two identical subunits. This enzyme was denatured in 6 M urea solution at pH 2.5, and kinetical analysis of reactivation by dilution was performed. At low protein concentrations a second-order kinetics for reactivation of phosphatase, with rate constant 8.3 m M-1sec-1, was observed. At higher protein concentrations the reactivation obeyed first-order kinetics. These results seem to exclude the possibility that subunits of the prostatic phosphatase are catalytically active and suggest that the association of two monomers is necessary for full activity.
前列腺酸性磷酸酶[E.C. 3.1.3.2.]是一种由两个相同亚基组成的二聚体蛋白。该酶在pH 2.5的6 M尿素溶液中变性，并通过稀释进行了复性动力学分析。在低蛋白浓度下，观察到磷酸酶复性的二级动力学，速率常数为8.3 mM-1sec-1。在较高蛋白浓度下，复性遵循一级动力学。这些结果似乎排除了前列腺磷酸酶亚基具有催化活性的可能性，并表明两个单体的缔合对于完全活性是必要的。
