蛋白质的分子结构对非线性声参量B／A的影响  

Influence of molecular structure of protein on acoustic nonlinearity parameter B/A

作　　者：鲁志劬[1] 龚秀芬[1] 王石泉[1] 

机构地区：[1]南京大学声学所,南京大学近代声学实验室,南京大学生化系

出　　处：《声学学报》1996年第5期783-789,共7页Acta Acustica

摘　　要：本文研究蛋白质分子结构对非线性声参量Ｂ／Ａ的影响，即由生化技术采用变性剂十二烷基硫酸钠（ＳＤＳ）溶液对三种蛋白质（牛血清蛋白、牛血红蛋白、胃蛋白酶）进行作用，以破坏其维持蛋白质空间构象的四、三、二级结构，而不改变其一级结构，也就是仅改变结构而不改变蛋白质的化学成份，用改进热力学法测量Ｂ／Ａ值受其影响的程度。实验结果表明：ＳＤＳ溶液浓度越大对蛋白质分子结构的破坏越严重，非线性参量Ｂ／Ａ中蛋白质的贡献就越小；Ｂ／Ａ能够反映蛋白质分子结构遭破坏的程度。该文对此现象作出一定的解释。In this papert the influence of molecular structure of protein on the acoustic nonlinearityparameter B/A has been studied. By using biochemical technique, three proteins (bovine serum albumin, bovine hemoglobin, pepsin) were employed and their secondary, tertiary and quarternary proteinstructures were perturbed by the denaturing agent sodium dodecyl sulfate (SDS) solution, while theirprimary structures of protein were not changed. This means that only the structural features werealtered and the chemical composition maintained unchanged. B/A have been measured by using improved thermodynamic method. The experimental results show that when the concentration of SDSsolution increases, the alterations of the protein structure increase, and the contribution of protein tothe B/A values decreases. Results indicate that the B/A values can display the destruction of molecular structure of protein. Some explanation of these phenomena has also been made in this paper.

关 键 词：蛋白质 分子结构 声能量 非线性声学 生物声学 

分 类 号：Q62[生物学—生物物理学]