从短杆菌JM98A中纯化一种内源性多核苷酸磷酸化酶。
Purification of an Endogenous polynucleotide phosphorylase from Brevibacterium JM98A.
作者信息
Yang H H, Thayer D W, Yang S P
出版信息
Appl Environ Microbiol. 1979 Jul;38(1):159-61. doi: 10.1128/aem.38.1.159-161.1979.
Abstract
Polynucleotide phosphorylase was purified form Brevibacterium JM98A (ATCC 29895). Homopolynucleotides were arsenolysed in the order polyadenylate greater than polycytidylic acid greater than polyuridylic acid greater than polyguanylate. The products were ribonucleoside 5'-monophosphates.
摘要
多核苷酸磷酸化酶是从短杆菌JM98A（美国典型培养物保藏中心29895）中纯化得到的。同聚核苷酸按多聚腺苷酸＞聚胞苷酸＞聚尿苷酸＞聚鸟苷酸的顺序被砷解。产物为核糖核苷5'-单磷酸。
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本文引用的文献
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Thermostable polynucleotide phosphorylases from Bacillus stearothermophilus and Thermus aquaticus.来自嗜热脂肪芽孢杆菌和嗜热水生栖热菌的热稳定多核苷酸磷酸化酶。
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Reduction of endogenous nucleic acid in a single-cell protein.降低单细胞蛋白中的内源性核酸。
Appl Environ Microbiol. 1979 Jul;38(1):143-7. doi: 10.1128/aem.38.1.143-147.1979.
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