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Adaptive Response of Expression of Soluable Proteins in Different Issues of Heilongjiang Ranidae under Stress of Low Temperature

Author: WangZuo
Tutor: XiaoXiangHong
School: Northeast Forestry University
Course: Physiology
Keywords: low temperature Northeast forest frog Frog muscle heart protein
CLC: Q51
Type: Master's thesis
Year: 2009
Downloads: 108
Quote: 0
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Abstract


The study aims to watch the changes on the muscle&heart soluble proteins of Northeast forest frog and Frog under low temperature,and finding out the relationship between the change rule of inner substance and cold tolerance.Its cold-tolerant mechanism has an important applied value,and a great potential for exploitation and utilization.The result:the frog’s survival ratio was 100%at 16℃and 4℃after 72h.Low temperature stress and survival ratio of Frog fell to 80%after 24h exposed at-2℃,Northeast forest frog is also 100%.This showed that the Northeast forest frog and Frog had longtime cold tolerance and short time freeze tolerance.Native PAGE separated proteins of muscle tissue successfully on the better condition is 6%final gel concentration.Northeast forest frog and Frog muscle protein band Rf=0.86 at 4℃and-2℃were significantly higher than at room temperature(P＜0.05);Northeast forest frog muscle protein band Rf=0.60 at-2℃was significantly higher than room temperature,and there was no change at 4℃.Frog muscle protein band Rf=0.74 at 4℃and-2℃were significantly lower than at room temperature.Native PAGE separated proteins of heart tissue successfully on the better condition is 10% final gel concentration and there were 11～17 bands identified on this condition.The content of one Northeast forest frog and Heiban frog muscle protein band(R_f=0.79)at 4℃and-2℃was significantly lower than at room temperature(P＜0.05),and R_f=0.86 was significantly higher than at room temerature(P＜0.05).On the muscle protein 10%2-D native-PAGE/SDS-PAGE gel,the content of D (MW=32kDa)at-2℃was significantly was lower than at room temperature(P＜0.05),and the content of E(MW=16 kDa)at-2℃was significantly higher than at room temperature.On the heart protein 10%2-D native-PAGE/SDS-PAGE gel,the content of A(MW=48kDa)at-2°C was significantly higher than at room temperature(P＜0.05),and the content of D (MW=28kDa)at-2°C was significantly lower than at room temperature(P＜0.05).The result indicate:the specificity change of muscle and heart protein at low temperature may

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CLC: > Biological Sciences > Biochemistry > Protein
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