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酶NADPH:原叶绿素酸酯氧化还原酶的前质体定位

Sub-etioplast localization of the enzyme NADPH: protochlorophyllide oxidoreductase.

作者信息

Lütz C, Röper U, Beer N S, Griffiths T

出版信息

Eur J Biochem. 1981 Aug;118(2):347-53. doi: 10.1111/j.1432-1033.1981.tb06409.x.

Abstract

The membranes from oat etioplasts have been separated by sucrose density gradient centrifugation into a heavy fraction of density 1.20 mg/ml (prolamellar body fraction) and a light fraction of density 1.12 mg/ml (prothylakoid fraction). The light fraction was shown to be enriched in protein, protochlorophyllide and the chloroplast enzyme CF1-ATPase, but to be deficient in saponins. In the electron microscope this fraction appeared as swollen vesicles. In contrast the heavy fraction appeared considerably enriched in crystalline, tubular material and was on analysis found to contain most of the etioplasts' saponin but with reduced protein and pigment. In the same experiments the enzyme NADPH: protochlorophyllide oxidoreductase showed the same distribution pattern as the CF1-ATPase suggesting its location on the prothylakoids.

摘要

燕麦黄化质体的膜已通过蔗糖密度梯度离心法分离成密度为1.20毫克/毫升的重组分(原片层体组分)和密度为1.12毫克/毫升的轻组分(原类囊体组分)。结果表明,轻组分富含蛋白质、原叶绿素酸酯和叶绿体酶CF1 - ATP酶,但皂苷含量不足。在电子显微镜下,该组分呈现为肿胀的囊泡。相比之下,重组分在晶体状、管状物质中含量明显丰富,经分析发现含有大部分黄化质体的皂苷,但蛋白质和色素含量降低。在相同实验中,酶NADPH:原叶绿素酸酯氧化还原酶显示出与CF1 - ATP酶相同的分布模式,表明其位于原类囊体上。

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