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Thermal stability and enzymatic activity of RNase A in the presence of cationic gemini surfactants.

Abstract：

:The thermal stability and enzymatic activity of bovine pancreatic ribonuclease A (RNase A) have been investigated in the presence of a homologous series of cationic gemini surfactants (alkanediyl-α,ω-bis(hydroxyethyl methyl hexadecyl ammonium bromide)). UV, circular dichorism and fluorescence spectroscopies have been used for this study. The denaturation curves at various surfactant concentrations were analyzed on basis of a two-transition model to obtain values of T(m) (temperature at the midpoint of denaturation) and ΔH(m) (enthalpy change at T(m)) of each transition. The main conclusion of this study is that these cationic gemini surfactants slightly activate and stabilize RNase A below their critical micelle concentrations at pH 5.0. The cationic gemini surfactant with the shorter spacer interacts more efficiently with RNase A than those with longer spacers.

journal_name

Int J Biol Macromol

journal_title

International journal of biological macromolecules

authors

Amiri R,Bordbar AK,Laurents DV,Khosropour AR,Mohammadpoor-Baltork I

doi

10.1016/j.ijbiomac.2012.01.027

subject

Has Abstract

pub_date

2012-05-01 00:00:00

pages

1151-7

issue

4

eissn

0141-8130

issn

1879-0003

pii

S0141-8130(12)00029-3

journal_volume

50

pub_type

杂志文章

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