Fluorescence quenching study on the interaction of Lycium barbarum polysaccharide with bovine serum albumin

被引：5

作者：

Zhang, Xianggang ^{[1
]}

Hao, Changchun ^{[1
]}

Nan, Zhezhu ^{[1
]}

Sun, Runguang ^{[1
]}

机构：

[1] Shaanxi Normal Univ, Sch Phys & Informat Technol, Xian 710062, Shaanxi, Peoples R China

来源：

APPLIED PHYSICS EXPRESS | 2019年 / 12卷 / 09期

基金：

中国国家自然科学基金;

关键词：

BINDING; SPECTROSCOPY; COMPLEX; BSA;

D O I：

10.7567/1882-0786/ab37ab

中图分类号：

O59 [应用物理学];

学科分类号：

摘要：

Fluorescence quenching was used to study the potential interaction mechanism of bovine serum albumin (BSA) with Lycium barbarum polysaccharide (LBP). Experimental results show that the quenching mechanism of BSA and LBP is static quenching. An ultraviolet spectrophotometer showed that the conformation of BSA changed with the addition of LBP. There is only one binding site between BSA and LBP and the binding site is tryptophan on BSA. And BSA and LBP are bonded together by a hydrogen bond. (C) 2019 The Japan Society of Applied Physics

引用

页数：6

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