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Kinetic behavior of associating enzyme systems ofthe type M in equilibrium M2 in equilibrium M3 in equilibrium ... and of the type 2M in equilibrium D in equilibrium D2 in equilibrium D3 in equilibrium ...
Molecular Biology ( IF 1.2 ) Pub Date : 1975-01-01
B I Kurganov

A theoretical analysis has been made of dependencies of specific enzymatic activity (a) on the concentration of the enzyme for associating enzyme systems, in which the association of protein molecules leads to the formation of linear associates of an unlimited length (M in equilibrium M2 in equilibrium M3 in equilibrium ...) and is accompanied by steric shielding of active centers, and also for systems of the type 2 M in equilibrium D in equilibrium D2 in equilibrium D3 in equilibrium ... (M is an inactive monomer and D is an active dimer), in which the specific enzymatic activity of the dimer does not depend on the degree of association. For both models an analysis has been made of the S-shape of the curves of the dependence of a on the concentration of the substrate. Experimental data for glutamate dehydrogenase from ox liver and phosphofructokinase from rabbit skeletal muscles have been used as illustrations.

中文翻译:

在平衡...中,平衡M2中的M型在平衡M3中的缔合酶系统的动力学行为,在平衡D3中在平衡D2的平衡D2中在平衡D的2M型酶体系的动力学行为...

对特定酶活性(a)对用于酶联系统的酶浓度的依赖性进行了理论分析,其中蛋白质分子的缔合导致无限长的线性缔合体的形成(平衡态M2中的M平衡M3处于平衡状态...),并伴随有活性中心的空间屏蔽,并且对于平衡D中处于平衡D2中的D类型处于平衡D2中处于平衡D3的系统...(M为非活性单体,D为(活性二聚体),其中二聚体的特定酶活性不取决于缔合程度。对于这两种模型,已经分析了α对底物浓度的依赖性的曲线的S形。
更新日期:2019-11-01
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