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首页> 外文期刊>Molecular and Cellular Biochemistry: An International Journal for Chemical Biology >Effects of hibernation on multicatalytic proteinase complex in thirteen-lined ground squirrels, Spermophilus tridecemlineatus
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Effects of hibernation on multicatalytic proteinase complex in thirteen-lined ground squirrels, Spermophilus tridecemlineatus

机译：冬眠对十三只内衬松鼠多精子线虫多催化蛋白酶复合物的影响

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摘要

Multicatalytic proteinase complex (MCP) was studied in skeletal muscle of the hibernating ground squirrel, Spermophilus tridecemlineatus. MCP was partially purified using a S-400 gel filtration column and Centricon concentrating devices and assayed fluorometrically using three AMC-labeled substrates. K-m and V-max values were determined for each substrate with no significant differences between the enzyme from euthermic versus hibernating animals when assayed at 23 degrees C. However, properties of MCP from euthermic and hibernating ground squirrels were differentially affected by low assay temperature (8-10 degrees C) and also differed from the mouse enzyme, the data indicating that ground squirrel MCP is better suited for low temperature function. MCP preferentially degrades oxidatively-damaged proteins and quantification of protein carbonyl content showed that the level of oxidatively-damaged protein in skeletal muscle decreased by > 75% during hibernation suggesting a continuing role for the MCP in the torpid state.
机译：研究了冬眠地松鼠Spermophilus tridecemlineatus骨骼肌中的多催化蛋白酶复合物（MCP）。使用S-400凝胶过滤柱和Centricon浓缩设备部分纯化MCP，并使用三种AMC标记的底物进行荧光分析。在23°C进行测定时，确定了每种底物的Km和V-max值，在正常动物和冬眠动物的酶之间没有显着差异。但是，低温和低温冬眠松鼠的MCP特性受测定温度低的影响（8 -10摄氏度）并且也不同于小鼠酶，数据表明地松鼠MCP更适合低温功能。 MCP优先降解氧化损伤的蛋白质，蛋白质羰基含量的定量显示，冬眠期间骨骼肌氧化损伤的蛋白质水平降低了> 75％，这表明MCP在in性状态下继续发挥作用。

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