Disulphide Bond Reduction of RNase A by Drug Metosartan a Comparative Study
Eswari Beeram *
Department of Biochemistry, Sri Venkateswara University, Tirupathi-517502, India.
Kamala Katepogu
Department of Biochemistry, Sri Venkateswara University, Tirupathi-517502, India.
Bukke Suman
Department of Biochemistry, Sri Venkateswara University, Tirupathi-517502, India.
Divya Bysani
Department of Biochemistry, Sri Venkateswara University, Tirupathi-517502, India.
Thyagaraju Kedam
Department of Biochemistry, Sri Venkateswara University, Tirupathi-517502, India.
*Author to whom correspondence should be addressed.
Abstract
RNase A is the most experimental protein in the 20th century. Disulphide bonds are necessary for enzymatic action of many proteins as it is also required for this protein. RNaseA kinetic studies is performed with the drug metosartan using RNA as the substrate Metosartan, is a drug used as blocker in excretion and found to contain inhibitory property on RNaseA. Protein degradation and thiol titration assay has found to be that the drug has reducing property on RNaseA.
Keywords: RNaseA, SDS PAGE, enzyme kinetics, beta blocker, Angiotensin receptor type I.