摘要
The interaction between BSA (Bovine Serium Albumin)and SDBS (Sodium Do-decyl Benzene sulfonate) at water - air interface of aqueous solution was investigated byADSA(Axisymmetric Drop Shape Analysis) method. The surface tension responses to time weremeasured and compared. The results showed that (1) ADSA is a good methed to study the dy-namic change of surface tellsion to the time; (2) While SDBS concentration was less than its CMC,it could interact with BSA macro-molecule in the solution to form a complex which was moresurface active than both BSA and SDBS, and its conformation change in the adsorption layer wassimilar with that of BSA alone, (3) While SDBS concentration was larger than its CMC, its micellecould solubilize the BSA macro-molecule and the surface tension and the conformation change inthe adsorption layer was very similar with these of SDBS solution alone.
The interaction between BSA (Bovine Serium Albumin)and SDBS (Sodium Do-decyl Benzene sulfonate) at water - air interface of aqueous solution was investigated byADSA(Axisymmetric Drop Shape Analysis) method. The surface tension responses to time weremeasured and compared. The results showed that (1) ADSA is a good methed to study the dy-namic change of surface tellsion to the time; (2) While SDBS concentration was less than its CMC,it could interact with BSA macro-molecule in the solution to form a complex which was moresurface active than both BSA and SDBS, and its conformation change in the adsorption layer wassimilar with that of BSA alone, (3) While SDBS concentration was larger than its CMC, its micellecould solubilize the BSA macro-molecule and the surface tension and the conformation change inthe adsorption layer was very similar with these of SDBS solution alone.
出处
《物理化学学报》
SCIE
CAS
CSCD
北大核心
1998年第7期649-653,共5页
Acta Physico-Chimica Sinica
基金
攀登计划
关键词
蛋白质
相互作用
BSA
SDBS
ADSA
表面活性剂
Drop shape analysis, Digital image process, Dynamic surface tension, Protein Interaction