This result proved that the inhibition of ventricular contractile purpose aurora inhibitorAurora A inhibitor by H2S was probably mediated by preventing the L type calcium channels. The substituted cysteine accessibility method was trusted to elucidate the features of ion channels. The oxidation states of the sulfhydryl groups of the cysteine containing peptides and proteins are crucial to stabilization of its composition and function, and an unique sulfhydryl modifier can localize functional regions of the molecule. Sulfhydryl reagents are crucial in SCAM. DTT is disulfide bonds that can be reduced by an effective sulfhydryl reductant irrespective of inter chain or intra chain linkages. DM is a commonly used sulfhydryl oxidizer if they are adjacent in the three dimensional structure of a protein as it can promote formation of a disulfide bridge between two cysteine residues. In our study we discovered that the L variety Ca currents were reduced by 1 mmol/L DM, and the decrease may be corrected by 5 mmol/L DTT, while either 1 mmol/L Plastid or 5 mmol/L DTT had no immediate effect on I Ca, L. These results suggest that the sulfhydryl groups on the M type Ca2 channels are very important gate sites that might be immediately changed by sulfhydryl reagents. L type calcium channel on membrane consists of a pore forming a1c subunit and regulatory a2, n and b sub-units. The subunit which determines the fundamental electrophysiological properties and influence being a receptor and voltage sensor for antagonists/agonists has free sulfhydryl groups, while disulfide bonds are present between your a2 and d subunits. DM provides an oxidative environment which can form a disulfide bridge to stabilize the 3d structure of the protein. For that reason, it may be proposed the formation of disulfide bonds within the a1 subunit is the site affected by DTT. Studies on D ethylmaleimide, chloramine T, 2, 2 dithiodipyridine Cyclopamine Hedgehog inhibitor and 2, 2 dithio bis 5 nitropyridine also showed a lowered impact on I Ca, L. Other results also indicated sulfhydryl reagents may immediately act to the ion channel, since the effect wasn’t because of either cAMP production or G protein coupled regulation of L form Ca2 stations. The current results confirmed that I Ca, L in the rat heart was restricted by H2S, and the thiol oxidant DM was observed to result in a decline in I Ca, L, and with pre experience of DM adopted by perfusion with H2S, the Ca2 current did not change compared with the get a grip on value. DTT had no direct effect on I Ca, L, though it could reverse the inhibition of I Ca, L by NaHS. Since free sulfhydryl groups on the L type Ca2 channels are the gate sites, and they may be immediately altered by hydrosulfuryl reagents, H2S would have no targeting site since DM would have already changed the oxidation state of the sulfhydryl groups of the L type Ca2 channels and formed a disulfide bridge between adjacent cysteine residues in the 3d structure.