scatchard analysis meaning in English
scatchard分析法
Examples
- Part i this paper has minutely studied the interaction between ag ( i ) and serum albumin . the binding of ag ( i ) to human serum albumin ( hsa ) or bovine serum albumin ( bsa ) has been studied by equilibrium dialysis at ph ( 5 . 4 ) . the scatchard analysis indicates that there exists several strong binding sites of ag ( i ) in both hsa and bsa . a notable hysteretic effect has been observed in the interaction of ag ( i ) with hsa or bsa using uv - visible spectrometry at ph ( 5 . 4 ) , which shows that the binding between ag ( i ) with hsa or bsa may induce a slow transition of hsa or bsa from the conformation of weaker affinity for ag ( i ) to one of stronger affinity ( a - b transition ) . the rate constants and activation parameters of this transition parameters of this tansition were measured and discussed . the binding equilibrium has been also studied by resonance light - scattering spectrum ( rls ) and flurescence quenching
第一部分：等离子点ph ( 5 . 4 )条件下，用平衡透析法和紫外光谱，荧光光谱，共振散射光谱研究了ag ( )与人血清白蛋白( humanserumalbumin ，简称hsa )或牛血清白蛋白( bovineserumalbumin ，简称bsa )的结合。 scatchard图分析表明， ag ( )在hsa或bsa中有强弱两类结合部位，通过计算机拟合获得结合的逐级稳定常数值。紫外扫描发现ag ( )与hsa或bsa的结合存在滞后效应，表明ag ( )与hsa或bsa的结合可能诱导蛋白质构象发生缓慢变化( a - b ) ，测得并讨论了这一构象变化的速度常数和活化参数。 - The internalization of oligochitosan in macrophage is a time - course process . 2 . initial experiments tested time , temperature , and concentration dependence of 2 - amac - oligochitosan uptake in macrophages . scatchard analysis of internalization of 2 - aminoacridone - oligochitosan in macrophages indicated its internalization is mediated by a specific receptor on macrophage membrane with ka of 2 . 1 10 - 5m
2 . 2一氨基叮睫酮标记的壳寡糖与巨噬细胞的结合是一个依赖时间、温度和浓度的过程， scatchard分析后发现它对巨噬细胞的作用是通过膜上特异性的受体( kd为2 . 1x10一sm )进行的。 - Part ii this paper has minutely studied the interaction between au ( iii ) and serum albumin . the binding of au ( iii ) to human serum albumin ( hsa ) or bovine serum albumin ( bsa ) has been studied by equilibrium dialysis at ph ( 7 . 43 + 0 . 02 ) . the scatchard analysis indicates that there exists several strong binding sites of au ( iii ) in both hsa and bsa . a notable hysteretic effect has been observed in the interaction of au ( iii ) with hsa or bsa using uv - visible spectrometry at ph ( 7 . 43 + 0 . 02 ) , which shows that the binding between au ( iii ) with hsa or bsa may induce a slow transition of hsa or bsa from the conformation of weaker affinity for au ( iii ) to one of stronger affinity ( a - b transition ) . the rate constants and activation parameters of this transition parameters of this tansition were measured and discussed . the binding equilibrium has project supported by the national science foundation of china ( no . 299621001 ) , and the foundation for talents of the ten hunred thousand in guangxi
第二部分：生理ph ( 7 . 43 0 . 02 )条件下，用平衡透析法和紫外光谱，荧光光谱研究了金( )与人血清白蛋白( humanserumalbumin ，简称hsa )或牛血清白蛋白( bovineserumalbumin ，简称bsa )的结合。 scatchard图分析表明，金( )在hsa或bsa中有强弱两类结合部位，通过计算机拟合获得结合的逐级稳定常数值。利用荧光猝灭法计算出金( ) - hsa和金( ) - bsa体系的stem - volmer常数和双分子猝灭速率常数。