Journal of Proteomics & Bioinformatics
Open Access

Reactivity of the CysF9[93]β of the sulphydryl group of the major horse (Equus caballus) haemoglobin

6^th International Conference & Expo on Proteomics

March 29-31, 2016 Atlanta, USA

Omolola E Omotosho, Shalom N Chinedu, Victor T Omotosho and Kehinde O Okonjo

Covenant University, Nigeria

Posters & Accepted Abstracts: J Proteomics Bioinform

Abstract :

The kinetics of the reaction of Ellmanâ��s reagent with CysF9[93]�² sulphydryl group of the horse hemoglobin were studied at neutral and physiological pH (6.87.6) ranges under pseudo first order conditions. The reaction is of first order with respect to the DTNB concentration in each plot. The reactions are pH dependent of the observed rate constant gave a complex trend. The observed rate shows that at neutral pH, the presence of inositol hexakisphosphate (inositol-P6) increases the pseudo first order rate constant. For the first time, inositol-P6 increases kF and kR at neutral pH values by increasing Krt3. The Krt3 for the haemoglobin without inositol-P6 gave the value of 0.138�±0.1 while the haemoglobin in the presence of inositol-P6 gave the Krt3 value of 0.325�±0.2. The results show that inositol-P6 increases the relative population of the t tertiary conformation. So, it increases the reactivity of CysF9[93]�² by changing the relative distribution of two protein conformations.

Biography :

Email: lola.omotosho@covenantuniversity.edu.ng