Identification of a guanine binding domain peptide of the GTP binding site of glutamate dehydrogenase: isolation with metal-chelate affinity chromatography.
Identification of a guanine binding domain peptide of the GTP binding site of glutamate dehydrogenase: isolation with metal-chelate affinity chromatography.
复制标题
谷氨酸脱氢酶 GTP 结合位点的鸟嘌呤结合域肽的鉴定：用金属螯合亲和层析分离。
DOI：
10.1021/bi00058a023
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发表时间：
1993
期刊：
影响因子：
2.9
通讯作者：
Haley,BE
中科院分区：
文献类型：
--
作者：
Shoemaker,MT;Haley,BE
材料与方法制备[7-32P] 8N3GTP和[«-32P] 8N3GTP （9-20 mCi/µ），按文献报道纯化（Geahlen & Haley, 1977; Potter & Haley, 1983）。通过Bio-Rad获得分子量标准。牛谷氨酸脱氢酶（GDH）、胰蛋白酶和凝乳胰蛋白酶及所有其他试剂均来自Sigma Chemical Co.，均为分析级。
MATERIALS AND METHODS [7-32P] 8N3GTP and [«-32P] 8N3GTP (9-20 mCi/µ) were prepared and purified as previously reported (Geahlen & Haley, 1977; Potter & Haley, 1983). Molecular weight standards were obtained from Bio-Rad. Bovine glutamate dehydrogenase (GDH), trypsin, and chymotrypsin and all other reagents were obtained from Sigma Chemical Co. and were analytical grade.