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(Solved) A partially purified plant protease preparation is 40% inactivated by treatment with p-hydroxymercuribenzoate (PHMB) and 100% inactivated by...


A partially purified plant protease preparation is 40% inactivated by treatment with p-hydroxymercuribenzoate (PHMB) and 100% inactivated by treatment with N- tosyl-L-lysine chloromethylketone (TLCK). When 14C-labeled TLCK is employed the loss of activity is accompanied by the incorporation of counts into two polypeptides, one that migrates at Mr 50,000 and another that migrates at Mr 35,000 upon SDS- PAGE. A. On the basis of these findings, which residues likely directly participate in the proteolytic reaction(s) catalyzed by this protease preparation? What assumptions must you make concerning the primary and secondary effects of these reagents in order to draw this(these) conclusion(s)? 0 +H N O 3 CH 2CI NH 0 02320 HoxH N-tosyl-L-lysine g chloromfitchlyretone p-hydroxymercuribenzoate (PHMB) CH3 B. Depict the reaction of an active site residue in the enzyme with PHMB. Depict the reaction of an active site residue in the enzyme with TLCK. D. How would you further test your proposal(s)? Again, explain your assumptions and any limitations inherent in the techniques you suggest. It will be particularly important to design an experiment or experiments that enable you to gain an indication of whether the residues you have invoked in the catalytic mechanism are dependent on each other or capable of acting independently (for instance, whether two different residues on the same or different polypeptides might participate in the same or different proteolytic reactions). 9
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Would like to be able to see if my logic and reasoning was correct here. No answers for 5 are given though.
This question was created from BIOL 204 (2016) Problem Set 3.pdf https://www.coursehero.com/file/13603267/BIOL-204-2016-Problem-Set-3pdf/?focusQaId=10550543

 


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