1. Sulfer hot springs are a common source of archaebacteria, the third domain of
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1. Sulfer hot springs are a common source of archaebacteria, the third domain of life that biohemically may to be more similar to eukaryotes than bacteria. You have just read research indicating that archaebacteria may be a rich source of a novel family of proteins, the Querall family. These proteins bind to selenium and activate other proteins through an unusual sulfhydryl modification of amines within the cell to repair telomeres, restore replicative ability, and as a result, reverse the aging process. Though they bind selenium, they seem to have a basic pl, in the range of 8.7-9.5. They also tend to be in the size range of the most common archae proteins, ranging from 10kDa to 90 kDa. Eager to begin your study, you've already set up your own aritificial hot spring and have a thriving culture of archaebacteria to sample. However, you now need to isolate the proteins.Explanation / Answer
An enzyme is a protein which shows discrete biological activities. When an appropriate substrate is present under suitable conditions of hydration, pH, temperature and concentrations of substrate and enzyme, there occurs bio-conversion reaction of substrate into products. It is very important to note here that the present information states that this enzyme/protein gets activated when it binds to selenium and confers further sulfhydryl modifications. This suggests that selenium is a crucial co-factor required for acquiring biological activity of this enzyme. The observation states that tandem MS data shows presence of protein but there is no biological activity present. Thus, in order to investigate the biological activity, following steps can be taken:
1. Providing co-factor: Since the information states that the protein recruites bio-chemical reaction only after binding to selenium, it is necessary to add selenium in exceedingly low concentrations in the reaction mixture. This can help in activation of the enzyme and thus, activity can be estimated.
2. Using an appropriate substrate and reaction conditions: It must be taken into account that this enzyme has been isolated from a bacteria residing in extreme conditions of temperature and pH. Thus, it is highly likely that activity of this enzyme will be obtained only at those specific conditions. Thus, it is very critical to mimic these environmental conditions in vitro to analyse the biological activity of the enzyme. For example, the enzyme Taq DNA polymerase obtained from bacteria Thermus aquaticus is stable at high temperature i.e. 90-100 degree celcius. Below these temperature grades, the enzyme is present and can be detected in the form of protein but its biological activity is absent.
Thus, following these trouble-shoots, the activity of this new enzyme can be analysed.
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