普通变形杆菌中嘌呤核苷磷酸化酶的纯化与特性分析
Purification and characterization of purine nucleoside phosphorylase from Proteus vulgaris.
作者信息
Surette M, Gill T, MacLean S
机构信息
Department of Food Science and Technology, Technical University of Nova Scotia, Halifax, Canada.
出版信息
Appl Environ Microbiol. 1990 May;56(5):1435-9. doi: 10.1128/aem.56.5.1435-1439.1990.
Abstract
Purine nucleoside phosphorylase was isolated and purified from cell extracts of Proteus vulgaris recovered from spoiling cod fish (Gadus morhua). The molecular weight and isoelectric point of the enzyme were 120,000 +/- 2,000 and pH 6.8. The Michaelis constant for inosine as substrate was 3.9 x 10(-5). Guanosine also served as a substrate (Km = 2.9 x 10(-5). However, the enzyme was incapable of phosphorylizing adenosine. Adenosine proved to be useful as a competitive inhibitor and was used as a ligand for affinity chromatography of purine nucleoside phosphorylase following initial purification steps of gel filtration and ion-exchange chromatography.
摘要
从变质鳕鱼（大西洋鳕鱼）中分离得到的普通变形杆菌细胞提取物中分离并纯化出嘌呤核苷磷酸化酶。该酶的分子量为120,000±2,000，等电点为pH 6.8。以肌苷为底物时的米氏常数为3.9×10⁻⁵。鸟苷也可作为底物（Km = 2.9×10⁻⁵）。然而，该酶无法磷酸化腺苷。腺苷被证明是一种有效的竞争性抑制剂，在经过凝胶过滤和离子交换色谱的初步纯化步骤后，被用作嘌呤核苷磷酸化酶亲和色谱的配体。
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