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豌豆超氧化物歧化酶的温度敏感性差异

Differential temperature sensitivity of pea superoxide dismutases.

作者信息

Burke J J, Oliver M J

机构信息

U.S. Department of Agriculture-Agricultural Research Service Cropping Systems Research Laboratory, Route 3, Box 215, Lubbock, Texas 79401.

出版信息

Plant Physiol. 1992 Nov;100(3):1595-8. doi: 10.1104/pp.100.3.1595.

Abstract

The activity of pea (Pisum sativum L.) Cu/Zn and Mn superoxide dismutase isoforms was evaluated across a range of temperatures from 10 to 45 degrees C. Maximal activity of the Cu/Zn and Mn superoxide dismutase isoforms was observed at 10 degrees C. Both cytoplasmic and chloroplast Cu/Zn superoxide dismutases exhibit a reduction in staining intensity with increasing temperatures. Mn superoxide dismutase, however, maintained a relatively constant staining intensity across the range of temperatures evaluated. An unrelated enzyme used as a control, malate dehydrogenase, exhibited the expected increase in staining activity with increasing temperatures. These results describe a unique response of a protection enzyme to temperature.

摘要

在10至45摄氏度的温度范围内评估了豌豆(Pisum sativum L.)铜/锌和锰超氧化物歧化酶同工型的活性。铜/锌和锰超氧化物歧化酶同工型的最大活性在10摄氏度时观察到。随着温度升高,细胞质和叶绿体铜/锌超氧化物歧化酶的染色强度均降低。然而,锰超氧化物歧化酶在评估的温度范围内保持相对恒定的染色强度。用作对照的一种不相关的酶,苹果酸脱氢酶,随着温度升高呈现出预期的染色活性增加。这些结果描述了一种保护酶对温度的独特反应。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6d48/1075828/1da429445795/plntphys00711-0523-a.jpg

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