RIBONUCLEOTIDE REDUCTASE ISOLATED FROM HUMAN CELLS - HETEROGENEITY AMONG SOURCES
RIBONUCLEOTIDE REDUCTASE ISOLATED FROM HUMAN CELLS - HETEROGENEITY AMONG SOURCES
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DOI：
10.1016/0006-2952(78)90134-x
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发表时间：
1978-01-01
影响因子：
5.8
通讯作者：
CHENG, YC
中科院分区：
文献类型：
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作者：
CHANG, CH;CHENG, YC
沉淀得自患者的组织细胞性淋巴瘤细胞或KB或Connaughton培养的人细胞的核糖核苷酸还原酶活性所需的硫酸铵的量不同于沉淀得自Molt-4F和HeLa S3细胞的还原酶活性所需的硫酸铵的量。Molt-4F细胞的还原酶活性在蔗糖密度梯度中以比KB细胞的酶活性更快的速率沉降。来自任一来源的CDP和ADP还原酶活性共沉积。酶从两个细胞系中的CDP和ATP的存在下，以更快的速度比在这些化合物的情况下，与CDP和ADP还原酶仍然共沉淀。从两种来源获得的酶在37 ℃下具有不同的稳定性。羟基脲、1-甲酰异喹啉缩氨基硫脲（IQ-1）、1，10-菲咯啉和KCl抑制Molt-4F或KB细胞的酶活性。观察到Molt-4F和KB细胞中CDP与ADP还原酶活性的比率的差异以及来自相同细胞系的CDP和ADP还原酶活性对不同浓度的抑制剂的敏感性之间的差异。核糖核苷酸还原酶作为癌症化疗的靶酶具有潜在的意义。
The amount of ammonium sulfate required to precipitate the ribonucleotide reductase activities derived from histiocytic lymphoma cells obtained from patients or from KB or Connaughton cultured human cells is different than for reductase activity derived from Molt-4F and HeLa S3 cells. The reductase activity of Molt-4F cells sedimented in a sucrose density gradient at a faster rate than the enzyme activity from KB cells. CDP and ADP reductase activity from either source co-sedimented. Enzymes from both cell lines sedimented at a faster rate in the presence of CDP and ATP than in the absence of these compounds, with CDP and ADP reductase still co-sedimenting. The enzymes obtained from the 2 sources have different stabilities at 37.degree.. Hydroxyurea, 1-formylisoquinoline thiosemicarbazone (IQ-1), 1,10-phenanthroline and KCl inhibit the enzyme activity derived from either Molt-4F or KB cells. A difference in the ratio of CDP to ADP reductase activity in Molt-4F and KB cells and a difference between the sensitivities of the CDP and the ADP reductase activities from the same cell line to various concentrations of inhibitors was observed. Ribonucleotide reductase is of potential interest as a target enzyme for cancer chemotherapy.