兔红细胞嘌呤核苷磷酸化酶。初速度研究。
Rabbit erythrocyte purine nucleoside phosphorylase. Initial-velocity studies.
作者信息
Savage B, Spencer N
出版信息
Biochem J. 1979 Apr 1;179(1):21-7. doi: 10.1042/bj1790021.
Abstract
- Concave-downward double-reciprocal plots were obtained for rabbit erythrocyte purine nucleoside phosphorylase when the concentration of Pi was varied over a wide range at a fixed saturating concentration of either inosine or deoxyinosine. Similar behaviour was also displayed by the calf spleen enzyme. 2. The degree of curvature of double-reciprocal plots was greatly modified by the presence of SO42-, introduced into the assay mixture with the linking enzyme xanthine oxidase; competitive inhibition by SO42- was observed over a narrow range of high Pi concentrations. 3. Partial inactivation with 5,5'-dithiobis-(2-nitrobenzoic acid) resulted in a marked alteration in the kinetic properties of the enzyme when Pi was the variable substrate. 4. Initial-velocity data are expressed in the form of Hill plots, and the significance of such plots is discussed.
摘要
- 当在肌苷或脱氧肌苷的固定饱和浓度下，将无机磷酸（Pi）的浓度在很宽的范围内变化时，得到了兔红细胞嘌呤核苷磷酸化酶的向下凹的双倒数图。小牛脾脏的酶也表现出类似的行为。2. 双倒数图的曲率程度因与连接酶黄嘌呤氧化酶一起引入测定混合物中的硫酸根离子（SO42-）的存在而大大改变；在高Pi浓度的狭窄范围内观察到SO42-的竞争性抑制。3. 用5,5'-二硫代双（2-硝基苯甲酸）部分失活导致当Pi为可变底物时酶的动力学性质发生明显改变。4. 初速度数据以希尔图的形式表示，并讨论了此类图的意义。
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