（ADP - 核糖）N糖苷水解酶在人红细胞中的存在情况。

Occurrence of (ADP-ribose)N glycohydrolase in human erythrocytes.

作者信息

Tanuma S, Kawashima K, Endo H

出版信息

Biochem Biophys Res Commun. 1986 May 14;136(3):1110-5. doi: 10.1016/0006-291x(86)90448-1.

Abstract

Chromatography of the cytosol of human erythrocytes on Blue Sepharose, S Sepharose, DEAE-cellulose and single-stranded DNA cellulose yielded a fraction which contained an (ADP-ribose)n glycohydrolase activity. The enzyme hydrolyzed (ADP-ribose)n in a fashion of exo-glycosidase. The native molecular weight of the enzyme was estimated to be 56,000 by gel filtration on Sepharose CL-6B. Its optimum pH was around 7.2. ADP-ribose, cAMP and monovalent salts inhibited the activity. Such characteristics established this glycohydrolase as being a cytosolic glycohydrolase II.

摘要

对人红细胞胞质溶胶在蓝色琼脂糖凝胶、S琼脂糖凝胶、二乙氨基乙基纤维素和单链DNA纤维素上进行色谱分析，得到了一个含有（ADP-核糖）n糖水解酶活性的组分。该酶以外切糖苷酶的方式水解（ADP-核糖）n。通过在琼脂糖CL-6B上进行凝胶过滤，估计该酶的天然分子量为56,000。其最适pH约为7.2。ADP-核糖、环磷酸腺苷和单价盐抑制该活性。这些特性确定这种糖水解酶为胞质溶胶糖水解酶II。