International Journal of Biochemistry Research & Review, ISSN: 2231-086X,Vol.: 20, Issue.: 1
Disulphide Bond Reduction of RNase A by Drug Metosartan a Comparative Study
Eswari Beeram1*, Kamala Katepogu1, Bukke Suman1, Divya Bysani1 and Thyagaraju Kedam1 1Department of Biochemistry, Sri Venkateswara University, Tirupathi-517502, India.
Eswari Beeram1*, Kamala Katepogu1, Bukke Suman1, Divya Bysani1 and Thyagaraju Kedam1
1Department of Biochemistry, Sri Venkateswara University, Tirupathi-517502, India.
(1) Halit Demir, Professor, Department of Chemistry, Faculty of Art and ScienceYuzuncu, Yil University, Turkey.
(1) Tatjana Momic, University of Belgrade, Serbia.
(2) Keagile Bati, University of Botswana, Botswana.
(3) Fellah Mamoun, Khenchela University, Algeria, And Annaba University, Algeria.
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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.
RNaseA; SDS PAGE; enzyme kinetics; beta blocker; Angiotensin receptor type I.
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