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变温动物酶的适应性特征——I. 温度对温带鱼类黄鳍连尾鮰苹果酸脱氢酶的影响

Adaptative features of ectothermic enzymes--I. Temperature effects on the malate dehydrogenase from a temperate fish Leiostomus xanthurus.

作者信息

Schwantes M L, Schwantes A R

出版信息

Comp Biochem Physiol B. 1982;72(1):49-58. doi: 10.1016/0305-0491(82)90009-8.

DOI:10.1016/0305-0491(82)90009-8
PMID:7105655
Abstract
  1. Following electrophoresis the s-MDH activity of Leiostomus xanthurus and many other species of fish and amphibian appears in three sharp, equally-spaced, anodal bands. Each band is a dimer (AA, AB and BB) and two loci are active. 2. In Leiostomus tissue extracts A and B subunits are present are differing quantitative levels and their activities can be modified by changes in environment temperature. 3. Thermostability and thermal dependency tests show that, similar to what occurs during acclimatization, the AA isozyme is more stable to heat than is the BB isozyme. The BB isozyme is activated by low temperatures and is rapidly inactivated by high temperatures. 4. Extracts from a variety of fishes, amphibians, reptiles and birds suggest that when only one or two s-MDH bands are present, they behave as dose the AA homodimer in Leiostomus Xanthurus, i.e., are stable at elevated temperatures.
摘要
  1. 电泳后,黄鳍连尾鮰以及许多其他鱼类和两栖类物种的可溶性苹果酸脱氢酶(s-MDH)活性呈现出三条清晰、等距的阳极条带。每条条带都是二聚体(AA、AB和BB),且有两个位点具有活性。2. 在黄鳍连尾鮰的组织提取物中,A和B亚基的含量不同,其活性会因环境温度的变化而改变。3. 热稳定性和热依赖性测试表明,与驯化过程中发生的情况类似,AA同工酶比BB同工酶更耐热。BB同工酶在低温下被激活,在高温下迅速失活。4. 来自各种鱼类、两栖类、爬行类和鸟类的提取物表明,当只存在一条或两条s-MDH条带时,它们的行为与黄鳍连尾鮰中的AA同型二聚体相同,即在高温下稳定。

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