41 The following data describe an enzyme-catalyzed reaction (hydrolysis of carbobenzoxyglycyl-L-tryptophan) Plot these results using the Lineweaver-Burk method, and determine values for KM and Vmax...


41 The following data describe an enzyme-catalyzed reaction (hydrolysis of<br>carbobenzoxyglycyl-L-tryptophan) Plot these results using the Lineweaver-Burk<br>method, and determine values for KM and Vmax<br>Velocity (mM.sec-)<br>0 024<br>0 036<br>0 053<br>0 060<br>0 061<br>0 062<br>Substrate Concentration (mM)<br>25<br>50<br>10 0<br>15 0<br>200<br>25 0<br>42 If the KM of an enzyme for its substrate remains constant as the concentration of the<br>inhibitor increases, what can be said about the mode of inhibition and why?<br>43 Calculate the turnover number for an enzyme, assumıng Vmax IS 05 M sec1 and the<br>concentration of the enzyme used is 0 002 M Why is it useful to know this?<br>44 Dıscuss the mechanism of the Bohr effect that occurs during the interactions of Hb<br>with oxygen under physiological conditions in the lungs and tissues Make use of<br>relevant graphs and diagrams to explain your answer<br>

Extracted text: 41 The following data describe an enzyme-catalyzed reaction (hydrolysis of carbobenzoxyglycyl-L-tryptophan) Plot these results using the Lineweaver-Burk method, and determine values for KM and Vmax Velocity (mM.sec-) 0 024 0 036 0 053 0 060 0 061 0 062 Substrate Concentration (mM) 25 50 10 0 15 0 200 25 0 42 If the KM of an enzyme for its substrate remains constant as the concentration of the inhibitor increases, what can be said about the mode of inhibition and why? 43 Calculate the turnover number for an enzyme, assumıng Vmax IS 05 M sec1 and the concentration of the enzyme used is 0 002 M Why is it useful to know this? 44 Dıscuss the mechanism of the Bohr effect that occurs during the interactions of Hb with oxygen under physiological conditions in the lungs and tissues Make use of relevant graphs and diagrams to explain your answer

Jun 11, 2022
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