Purification and Properties of Poly(A) Polymerase from Vigna unguiculata
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概要
- 論文の詳細を見る
Poly(A) polymerase was purified from germinating Vigna unguiculata seeds by successive column chromatography on phosphocellulose, Toyopearl HW-55S, heparin-Sepharose and TSKgel phenyl-5PW, which yielded two activity fractions. The first fraction was purified as a single polypeptide with a mol wt of 63,000 as estimated by SDS-PAGE. The enzyme activity was highly specific for ATP and required Mn^<2+> ion; an ATP-Mn complex may be the actual substrate. The polymerization reaction required a primer, with various types of RNAs, poly(A) as well as dinucleoside phosphates having 3'-OH, serving as efficient primers. The two forms of the enzyme had very similar properties with respect to divalent cation requirement and dependency on ion strength, but they showed some difference in primer preference.
- 日本植物生理学会の論文
著者
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Minamikawa Takao
Department Of Biological Sciences Tokyo Metropolitan University
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Tarui Y
Tokyo Metropolitan Univ. Tokyo Jpn
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Tarui Yutaka
Department Of Biology And Geology Graduate School Of Science Osaka City University
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Minamikawa Takao
Departmen T Of Biology Tokyo Metropolitan University
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