Adsorption kinetics and dilatational rheological studies for the soluble and anchored forms of alkaline phosphatase at the air/water interface
Adsorption kinetics and dilatational rheological studies for the soluble and anchored forms of alkaline phosphatase at the air/water interface
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DOI：
10.1590/s0103-50532005000600013
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发表时间：
2005-10
影响因子：
1.4
通讯作者：
L. Caseli;D. Masui;R. P. Furriel;F. A. Leone;M. D. Zaniquelli
中科院分区：
文献类型：
--
作者：
L. Caseli;D. Masui;R. P. Furriel;F. A. Leone;M. D. Zaniquelli
本研究介绍了两种大鼠骨板碱性磷酸酶形式在空气/液体界面吸附的平衡和动态方面：DSAP，由表面活性剂C12E9溶解，含有糖基磷脂酰肌醇（GPI）锚点；和PLSAP，由磷脂酶c切割GPI锚的疏水部分而产生。采用谐波振荡和轴对称滴形分析方法测定了PLSAP、DSAP和纯C12E9溶液的动态表面张力gdyn和表面弹性模量e。吸附动力学研究表明，DSAP的吸附速度比PLSAP快30倍，在曲线上呈现最小值。对于DSAP/ C12E9混合体系，e随浓度增加而增大，在临界聚集浓度（CAC）处出现最大值。PLSAP随着gdyn和e浓度的增加呈下降趋势。对于纯C12E9溶液，其弹性模量随浓度的增加而增大，且e值高于混合体系。提出了一种基于GPI锚点影响的模型。
This work presents equilibrium and dynamic aspects for the adsorption at the air/liquid interface of two rat osseous plate alkaline phosphatase forms: DSAP, solubilized by a surfactant, C12E9, and containing a glycosylphosphatidylinositol (GPI) anchor; and PLSAP, resulting from phospholipase-C cleavage of the hydrophobic portion of the GPI anchor. Dynamic surface tension, gdyn, and surface elasticity modulus, e, were determined for PLSAP, DSAP and pure C12E9 solutions using harmonic oscillation and axisymmetric drop shape analysis Adsorption kinetics studies revealed that DSAP adsorbs thirty times faster than PLSAP, presenting a minimum in the curve. For DSAP/ C12E9 mixed system, e increases with concentration and a maximum appears at the critical aggregation concentration (CAC). For PLSAP, a continuous decreasing with concentration for gdyn and e was observed. For pure C12E9 solution, the elasticity modulus increases with concentration and e values are higher when compared to the mixed system. A model based on the influence of the GPI anchor is proposed.