Study on the interaction between methyl violet and bovine serum albumin by spectral analyses.
In this article the interaction between methyl violet (MV) and bovine serum albumin (BSA) was studied with spectroscopy. The results indicated that the fluorescence intensity of BSA was quenched strongly by MV through a static quenching procedure. The association constants, the number of binding sites and basic thermodynamic parameters were obtained based on fluorescence quenching data. The effect of MV on the conformation of BSA had been investigated with synchronous fluorescence spectroscopy and circular dichroism (CD) spectrum.
Hu
Yanyan
Y
Department of Chemistry, Yangzhou University, Yangzhou 225002, Jiangsu, PR China.
Xu
Suqin
S
Zhu
Xiashi
X
Gong
Aiqin
A
D000818:Animals; D001665:Binding Sites; D002417:Cattle; D002942:Circular Dichroism; D005840:Gentian Violet / Q000032:analysis / Q000378:metabolism*; D011485:Protein Binding; D012710:Serum Albumin, Bovine / Q000032:analysis / Q000378:metabolism*; D013050:Spectrometry, Fluorescence; D013816:Thermodynamics
D012710:Serum Albumin, Bovine; D005840:Gentian Violet