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鸟氨酸氨甲酰基转移酶的前体作为一种包含导入因子的5S复合物被转运到线粒体。

The precursor to ornithine carbamyl transferase is transported to mitochondria as a 5S complex containing an import factor.

作者信息

Argan C, Shore G C

出版信息

Biochem Biophys Res Commun. 1985 Aug 30;131(1):289-98. doi: 10.1016/0006-291x(85)91801-7.

Abstract

The precursor to ornithine carbamyl transferase (Mr = 40,000) was synthesized in a rabbit reticulocyte lysate system and purified by immunoaffinity chromatography. Import of purified precursor by isolated mitochondria depended upon the presence of import factor(s) in fresh reticulocyte lysate. Velocity sedimentation analyses indicated that import factor binds to precursor to form a 5S complex (approximately 90 kDa); in this form, precursor was efficiently imported by isolated mitochondria. The ability of the 5S complex to deliver precursor into mitochondria was not affected by pretreatment with high concentrations of RNase. Import factor did not bind to mitochondria in the absence of precursor; upon binding of precursor to mitochondria in the presence of import factor, subsequent transmembrane uptake of precursor did not require the continued presence of additional lysate components.

摘要

鸟氨酸氨甲酰转移酶的前体(分子量 = 40,000)在兔网织红细胞裂解物系统中合成,并通过免疫亲和层析进行纯化。分离的线粒体对纯化前体的导入依赖于新鲜网织红细胞裂解物中导入因子的存在。速度沉降分析表明,导入因子与前体结合形成5S复合物(约90 kDa);以这种形式,前体可被分离的线粒体有效导入。5S复合物将前体递送至线粒体的能力不受高浓度核糖核酸酶预处理的影响。在没有前体的情况下,导入因子不与线粒体结合;在前体在导入因子存在下与线粒体结合后,前体随后的跨膜摄取不需要其他裂解物成分的持续存在。

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