Need for drawing graphs for the specific activity of alkaline phosphatase? thatguybil have the explanation for competitive inhibition correct. The Km will decrease as concentration of the inhibitor increases, but Vmax will across the world not change.
In the travel case of uncompetitive inhibition, the apparent Vmax and Km will both condense as the concentration of inhibitor increases. Unlike noncompetitive inhibitors, which bind both the enzyme and the ezyme-substrate complex, uncompetitive inhibitors bind only to the enzyme-substrate complex.
I will not report to you specifically for AlkPhos but I will explain the general rule.
competitive inhibitors can be overwhelmed next to more reagent thus Vmax does not change but Km does
Non competitive inhibitors works by occupy some other site on the enzyme thus they lower Vmax but do not change binding affinity (Km)
You can amount out what you need from that.
Vmax advantage reduce and does not metamorphose, where as Km change.
Enzyme kinetics reaction proves itself for Alkaline Phosphatase.
Subscribe to:
Post Comments (Atom)
No comments:
Post a Comment