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兔核糖体系统中的血红蛋白合成:血红素合成酶活性的定位

Hemoglobin synthesis in a rabbit ribosomal system: localization of heme synthetase activity.

作者信息

Gribble T J, Edmunds D, Schwartz H C

出版信息

Pediatr Res. 1977 Oct;11(10 Pt 2):1106-8.

PMID:904976
Abstract

The activity of heme synthetase (ferrochelatase), the enzyme(s) which catalyzes the formation of heme from iron and protoporphyrin IX, was studied in the various fractions of a cell-free reticulocyte system which synthesizes hemoglobin. The ribosomal fraction contained heme synthetase activity and its characteristics were similar to that described in avian erythrocytes, human and rat liver, and rabbit reticulocytes. It has a pH optimum of 7.5, required sulfhydryl reagents, was denatured by heat and was unstable on freezing. Heme synthetase is a mitochondrial enzyme. Fragments of mitochondrial membrane were identified in the ribosome fraction by both electron microscopy and the presence of cytochrome oxidase activity.

摘要

血红素合成酶(亚铁螯合酶)是一种催化铁和原卟啉IX形成血红素的酶,在合成血红蛋白的无细胞网织红细胞系统的各个组分中对其活性进行了研究。核糖体组分含有血红素合成酶活性,其特性与在鸟类红细胞、人和大鼠肝脏以及兔网织红细胞中所描述的相似。它的最适pH为7.5,需要巯基试剂,受热会变性,冷冻时不稳定。血红素合成酶是一种线粒体酶。通过电子显微镜和细胞色素氧化酶活性的存在,在核糖体组分中鉴定出线粒体膜碎片。

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