STUDIES ON NUCLEAR EXORIBONUCLEASES .3. ISOLATION AND PROPERTIES OF ENZYME FROM NORMAL AND MALIGNANT TISSUES OF MOUSE
STUDIES ON NUCLEAR EXORIBONUCLEASES .3. ISOLATION AND PROPERTIES OF ENZYME FROM NORMAL AND MALIGNANT TISSUES OF MOUSE
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DOI：
10.1021/bi00832a053
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发表时间：
1969-01-01
期刊：
影响因子：
2.9
通讯作者：
HENDERSON, WR
中科院分区：
文献类型：
--
作者：
SPORN, MB;LAZARUS, HM;HENDERSON, WR
Michael B. Sporn, Harrison M. Lazarus, f Joseph M. Smith和William R. Henderson摘要：从小鼠肝脏、肾脏、胚胎、乳腺肿瘤和埃利希腹水肿瘤的细胞核中分离到一种能将单链核糖核酸降解为核苷5'-单磷酸的外核糖核酸酶。通过50℃加热和3.2 m尿素处理使酶失活。这种酶对多核糖核苷酸具有特异性；它不会水解脱氧核糖核酸，pTpT或胸苷5 '-对硝基苯基磷酸。对多核糖核苷酸攻击机理的研究表明：(1)酶（从3'-OH端降解）催化
Michael B. Sporn, Harrison M. Lazarus, f Joseph M. Smith, and William R. Henderson abstract: An exoribonuclease, which degrades singlestranded ribonucleic acid to nucleoside 5'-mono-phosphates, has been isolated from the nuclei of mouse liver, kidney, embryo, mammary tumor, and Ehrlich ascites tumor. The enzyme is inactivated by heating at 50 and treatment with 3.2 m urea. The enzyme is specific for polyribonucleotides; it will not hydrolyze deoxyribonucleic acid, pTpT, or thymidine 5'-p-nitrophenylphosphate. Studies on the mechanism of attack on polyribonucleotides show that:(1) the enzyme (which degrades from the 3'-OH end) catalyzes