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热带禾本科牧草中羧化酶及其他酶的活性与光合二氧化碳固定新途径的比较研究

Comparative studies on the activity of carboxylases and other enzymes in relation to the new pathway of photosynthetic carbon dioxide fixation in tropical grasses.

作者信息

Slack C R, Hatch M D

出版信息

Biochem J. 1967 Jun;103(3):660-5. doi: 10.1042/bj1030660.

Abstract
  1. The activity per unit of chlorophyll of certain carboxylases, and of other enzymes involved in photosynthesis, was determined in leaf extracts of the tropical grasses, sugar-cane, maize and sorghum, and compared with the activities for wheat, oat and silver-beet. Maximum rates of photosynthetic carbon dioxide uptake were also measured for comparison with enzyme activities. 2. Phosphopyruvate carboxylase activity was about 60 times greater in the tropical grasses than in wheat, oat and silver-beet and was severalfold higher than the rates of photosynthetic carbon dioxide uptake. Most of the enzyme was located in the chloroplast fraction of cell extracts. 3. Phosphopyruvate carboxylase was apparently the major photosynthetic carbon dioxide-fixing enzyme in the tropical grasses, although malic enzyme may contribute to a lesser extent. 4. Tropical grasses contained less than one-tenth of the ribulose diphosphate carboxylase activity present in wheat, oat and silver-beet. For the tropical grasses this activity, determined with a saturating concentration of bicarbonate, was approx. 10% of the rate of photosynthesis. 5. The fraction-1 protein content of leaf extracts paralleled the ribulose diphosphate carboxylase activity. 6. In contrast, the activity of several other enzymes of the Calvin cycle was similar in the different species examined.
摘要
  1. 测定了热带禾本科植物甘蔗、玉米和高粱叶片提取物中某些羧化酶以及其他参与光合作用的酶的单位叶绿素活性,并与小麦、燕麦和甜菜的酶活性进行了比较。还测量了光合二氧化碳吸收的最大速率,以便与酶活性进行比较。2. 热带禾本科植物中磷酸丙酮酸羧化酶的活性比小麦、燕麦和甜菜高约60倍,且比光合二氧化碳吸收速率高出几倍。大部分酶位于细胞提取物的叶绿体部分。3. 磷酸丙酮酸羧化酶显然是热带禾本科植物中主要的光合二氧化碳固定酶,尽管苹果酸酶的贡献较小。4. 热带禾本科植物中核酮糖二磷酸羧化酶的活性不到小麦、燕麦和甜菜的十分之一。对于热带禾本科植物,在碳酸氢盐饱和浓度下测定的该活性约为光合作用速率的10%。5. 叶片提取物中1-类蛋白的含量与核酮糖二磷酸羧化酶的活性平行。6. 相比之下,在所研究的不同物种中,卡尔文循环的其他几种酶的活性相似。
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ffd7/1270465/9139fb179bdb/biochemj00742-0062-a.jpg

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