The Function Of S-nitrosylation In Peach Proteins And The Detection Of S-nitrosothiols By Surface Plasmon Resonance

As a simple signal molecule, nitric oxide widely exists in the organism. Giving the uniqueand important biological activities, NO plays a key role in regulating various processes. It wasfound that some specific sulfydryl group in protein can react with NO, resulting in theproduction of S-nitrosothiols. Therefore, it is of great help for us to study the process of signaltransduction.In this paper, Feicheng peach was used as the materials. The activity of SDH wasresearched by some biological and genomics methods. Site-directed mutation was applied forprobing the changes of SDH caused by NO. What is more,the mechanism of SDH activitywas also discussed later.The activity of SDH in peach fruits was controlled by the GSH/GSNO according to theresearch. Sometime, the content of NO rises because of external stimuli. Then the reducingsubstances such as DTT or GSH can react with NO resulting in the production ofS-nitrosothiols. At the same time, Zn2+can release from the activity center. In another way,DTT or GSH can directely reduce S-nitrosothiols releasing the free thiol group. As a result,the activity of SDH can be changed according to the content of ROS and RNS.Now, large number of biological method was used for the detection of S-nitrosylation.However,considering experimental period and expence, we can not put these methods intowidely use. As a new method, Surface plasmon resonance can be used in lots of parts shcu asprotein-protein interaction, DNA, cell apoptosis and others. Therefore, it may be a goodchoice that combing SPR and traditional biological method to probe S-nitrosylation.In this paper, Self-assemble monolayer basing on the golden flat was made to detect therelease of S-nitrosothiols.The results showed that the S-nitrosylation of BSA can beresearched.