[士的宁与牛血清白蛋白之间的相互作用]

[Interaction between strychnine and bovine serum albumin].

作者信息

Zhao Jin, Wang Zhi, Wu Qiu-hua, Yang Xiu-min, Wang Chun, Hu Yan-xue

机构信息

College of Food Science and Technology, University of Hebei, Baoding 071000, China.

出版信息

Yao Xue Xue Bao. 2006 Jul;41(7):666-70.

PMID:17007362

Abstract

AIM

To study the interaction between strychnine and bovine serum albumin.

METHODS

Fluorescence spectroscopy and ultraviolet spectroscopy were used.

RESULTS

The static quenching and the non-radiation energy transfer are the two main reasons to leading the fluorescence quenching of BSA. The apparent combining constants (K(A)) between strychnine and BSA are 3.72 x 10(3) at 27 degrees C, 4.27 x 10(3) at 37 degrees C, 4.47 x 10(3) at 47 degrees C and the combining sites are 1.01 +/- 0.03. The combining distance (r = 3.795 nm) and energy transfer efficiency (E = 0.0338) are obtained by Förster's non-radiation energy transfer mechanism.

CONCLUSION

The interaction between strychnine and BSA was driven mainly by hydrophobic force.

摘要

目的

研究士的宁与牛血清白蛋白之间的相互作用。

方法

采用荧光光谱法和紫外光谱法。

结果

静态猝灭和非辐射能量转移是导致牛血清白蛋白荧光猝灭的两个主要原因。士的宁与牛血清白蛋白之间的表观结合常数（K(A)）在27℃时为3.72×10(3)，37℃时为4.27×10(3)，47℃时为4.47×10(3)，结合位点为1.01±0.03。通过Förster非辐射能量转移机制得到结合距离（r = 3.795 nm）和能量转移效率（E = 0.0338）。