Determination of Sulphydryl and Disulphide Groups in Lysozyme
Harikrishna Yadav. Nanganuru1, Enzo Polambo2

1Harikrishna Yadav. Nanganuru, Swinburne University of Technology, Melbourne, Australia.
2Enzo Polambo, Associate Professor, Swinburne University of Technology, Melbourne, Australia.

Manuscript received on 07 February 2013 | Revised Manuscript received on 21 February 2013 | Manuscript Published on 28 February 2013 | PP: 149-153 | Volume-2 Issue-3, February 2013 | Retrieval Number: C0473022313/2013©BEIESP
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Abstract: Proteins contain several actual or potential sulfhydryl groups. These groups are very important for cellular respiration. A remarkable method of altering many proteins is to dissolve them in urea or other amide solutions. When a protein is partially denatured, that means only part of it is converted into a form insoluble under conditions under which the native protein is soluble, the insoluble fraction has the number of reactive SH and S-S groups characteristic of completely denatured protein, whereas the soluble fraction has the number characteristic of protein which has not been denatured at all. Finally, when a protein is converted by urea into a form which has an increased number of S-S groups, that form is insoluble in a medium in which native protein is soluble. In denaturation, formation of insoluble protein and increase in detectable SH and S-S groups are closely related aspect. The sulphide groups in the protein with DTNB in the tubes of 1, 2 and 3 having 1.365moles, 6.588moles and 0.158 moles respectively. Disulphide fluorescence quenching assay gives the number of moles of disulphide groups per mole of protein of the lysozyme was 10.4nmoles.
Keywords: Lysozyme, Cary Eclipse, Fluorescence Quenching Assay and Bovine Serum Albumin

Scope of the Article: Wireless Sensor Network