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[大肠杆菌K-12尿苷磷酸化酶的四级结构]

[Quaternary structure of uridine phosphorylase from E. coli K-12].

作者信息

Tsuprun V L, Tagunova I V, Lin'kova E V, Mironov A S

出版信息

Biokhimiia. 1991 May;56(5):930-4.

PMID:1747419
Abstract

Uridine phosphorylase was isolated from E. coli K-12 cells in a homogeneous state. The molecular mass of the enzyme as determined by gel filtration corresponds, approximately, to a hexamer made up of 27.5 kDa monomers. Evidence for the hexameric structure of uridine phosphorylase was obtained by electron microscopy with numerical treatment of the images. The six monomers within the enzyme molecule are arranged in two layers, three monomers in each, at the apices of a triangular antiprism with a point group symmetry of 32.

摘要

尿苷磷酸化酶以均一状态从大肠杆菌K-12细胞中分离出来。通过凝胶过滤测定的该酶分子量约相当于由27.5 kDa单体组成的六聚体。通过电子显微镜及图像数值处理获得了尿苷磷酸化酶六聚体结构的证据。酶分子内的六个单体排列成两层,每层三个,位于具有32点群对称性的三角反棱柱的顶点处。

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