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mundana衣藻光合能力的调控

Regulation of Photosynthetic Capacity in Chlamydomonas mundana.

作者信息

Russell G K, Gibbs M

机构信息

Department of Biology, Brandeis University, Waltham, Massachusetts.

出版信息

Plant Physiol. 1966 May;41(5):885-90. doi: 10.1104/pp.41.5.885.

DOI:10.1104/pp.41.5.885
PMID:16656335
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1086441/
Abstract

A regulatory system has been described in the obligately phototrophic green alga Chlamydomonas mundana. Cells grown in acetate media are unable to fix carbon dioxide in the light but carry out a photoassimilation of acetate to carbohydrate: cells cultured with carbon dioxide as the sole source of cellular carbon carry out typical green plant photosynthesis. The control appears to take place at the level of the reductive pentose phosphate cycle. The presence of sodium acetate in the medium strongly inhibits formation of ribulose-1.5-diphosphate carboxylase, ribulose-5-phosphate kinase, and one of the 2 fructose-1,6-diphosphate aldolase activities of the cell. Ribose-5-phosphate isomerase is present in higher activity in autotrophic cells. Changes in the levels of triose phosphate dehydrogenase were also noted. The total pigment content of the cell and the photosynthetic electron transport reactions are not altered under different conditions of growth.

摘要

在专性光合绿藻蒙氏衣藻中已描述了一种调节系统。在醋酸盐培养基中生长的细胞在光照下无法固定二氧化碳,但能将醋酸盐光同化形成碳水化合物:以二氧化碳作为细胞碳唯一来源培养的细胞进行典型的绿色植物光合作用。这种调控似乎发生在还原性戊糖磷酸循环水平。培养基中醋酸钠的存在强烈抑制细胞中1,5 - 二磷酸核酮糖羧化酶、5 - 磷酸核酮糖激酶以及两种果糖 - 1,6 - 二磷酸醛缩酶活性之一的形成。5 - 磷酸核糖异构酶在自养细胞中的活性较高。还注意到磷酸丙糖脱氢酶水平的变化。在不同生长条件下,细胞的总色素含量和光合电子传递反应未发生改变。

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本文引用的文献

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Intracellular and Phylogenetic Distribution of Ribulose 1,5-Diphosphate Carboxylase and D-Glyceraldehyde-3-Phosphate Dehydrogenases.1,5-二磷酸核酮糖羧化酶与3-磷酸甘油醛脱氢酶的细胞内分布及系统发育分布
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MITOTIC REPLICATION OF DEOXYRIBONUCLEIC ACID IN CHLAMYDOMONAS REINHARDI.莱茵衣藻中脱氧核糖核酸的有丝分裂复制
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A mutant strain of Chlamydomonas reinhardi lacking ribulose diphosphate carboxylase activity.莱茵衣藻的一种缺乏核酮糖二磷酸羧化酶活性的突变菌株。
Proc Natl Acad Sci U S A. 1965 May;53(5):987-90. doi: 10.1073/pnas.53.5.987.