黄素蛋白猪肾D-氨基酸氧化酶的缔合-解离。单体-二聚体平衡常数的测定及亚基缔合的能量学研究。
Association-dissociation of the flavoprotein hog kidney D-amino acid oxidase. Determination of the monomer-dimer equilibrium constant and the energetics of subunit association.
作者信息
Horiike K, Shiga K, Nishina Y, Isomoto A, Yamano T
出版信息
J Biochem. 1977 Nov;82(5):1247-55. doi: 10.1093/oxfordjournals.jbchem.a131812.
Abstract
The enzyme concentration dependence of spectrophotometric titrations of hog kidney D-amino acid oxidase [EC 1.4.3.3] with p-aminobenzoate was studied. The monomer-dimer equilibrium constant of the oxidized holoenzyme at 25 degrees C was estimated to be 7 X 10(5)M-1 at pH 7.5 and 4X 10(6)M-1 at pH 8.3. The energetics of subunit association are discussed.
摘要
研究了用对氨基苯甲酸对猪肾D-氨基酸氧化酶[EC 1.4.3.3]进行分光光度滴定的酶浓度依赖性。在25℃下，氧化型全酶的单体-二聚体平衡常数在pH 7.5时估计为7×10⁵M⁻¹，在pH 8.3时为4×10⁶M⁻¹。讨论了亚基缔合的能量学。
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