February 27th update

Hey everyone

Sorry for this post being a little late, I have the bad habit of saving posts and publishing them on different days! One basically assumes that saving will make it visible but it doesnt!
Up to the moment research in the lab has been slow. I had ordered some new sensor sleeves at the beginning of the semester and they have not yet arrived. So, at the moment I have achieved some progress but not much with regards to this semesters goals. Hopefully by the end of this week or the beginning of the following week, I will have received the materials that I am lacking. Although this has slowed me down, it doesnt mean I havent had my hands full at the moment. With this I mean that, this semester the laboratory has received 11 NEW undergraduate students that will be researching for college credit! For the past month I have been training them in laboratory protocol and I have trained many in the area of sulfmyoglobin. So, all is not lost yet!
Laboratory research has been a very rewarding experience but I am noticing the difficulties and intricacies it implies. From stocking reactives to ensuring the proper functioning of laboratory equipment, a lot of time can be lost in the efforts to make sure that each of these is up to par. I am also preparing to present at PRISM, meaning that my free time is pretty slim at the moment. Since we are supposed to publish an abstract of our research I have decided to publish the abstract that I sent to PRISM. It includes the description of last semester’s research experience, goals and results: It is as goes…

Abstract
Experimentation consisted of a kinetic analysis of the reactivity of hydrogen sulfide with myoglobin. The purpose of such experiment was to determine the formation constant of sulfmyoglobin (k1), a product of the reaction of myoglobin in presence of O2 or H2O2. This was accomplished by studying the kinetics of the reaction at different concentrations of H2S. The oxidation state of the myoglobin was a mixture of metaquo-myoglobin and oxy-myoglobin. The experimental concentrations of H2S were determined with the aid of the Apollo Free Radical Analyzer. The kinetic study consisted of treating equine myoglobin with H2S at the following proportions: 1:1, 1:2, 1:3, 1:4 and 1:5. In each reaction, the concentration of myoglobin remained constant at [15µM] while the [H2S] was altered. The reactions were conducted in presence atmospherical oxygen. The concentrations of two reagents remained constant (Mb and O2). Each reaction was spectrally analyzed for 38min and individual spectra were taken at 2min intervals. Special interest was given to the red region of the spectra (≈616-620nm) since it houses the unique sulfmyoglobin absorption band. Further analysis revealed that the small value of the formation constant (k1) was representative of a slow reaction rate. The value of the formation constant of sulfmyoglobin (k1) was 0.643654004 s-1M-1.

~ by chrismolini on March 2, 2009.