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网织红细胞释放因子的特性分析。

Characterization of reticulocyte release factor.

作者信息

Konecki D S, Aune K C, Tate W, Caskey C T

出版信息

J Biol Chem. 1977 Jul 10;252(13):4514-20.

PMID:873902
Abstract

The release factor (RF) of reticulocytes has been purified to greater than 75% homogeneity. The RF has a native molecular weight of 105,000 and subunit molecular weight of 56,500. The RF protein will bind to reticulocyte ribosomes in response to UAAA, UAGA, or UGAA and therefore participates in codon recognition. The fraction possess a ribosome-dependent GTPase activity. The RF is stimulated in its activity by a second protein fraction.

摘要

网织红细胞释放因子(RF)已被纯化至均一性大于75%。该RF的天然分子量为105,000,亚基分子量为56,500。RF蛋白会响应UAAA、UAGA或UGAA与网织红细胞核糖体结合,因此参与密码子识别。该组分具有核糖体依赖性GTP酶活性。RF的活性受到第二种蛋白质组分的刺激。

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