By L Indira; K Nagaraju; Zameer Ahmed K
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Additional info for College biochemistry. / VI
19. Describe the method used for the extraction of enzyme. 20. Define the following; (a) Enzyme activity (b) International unit (c) Specific activity (d) Turnover number 21. What is meant by enzyme kinetics? 22. Explain the kinetics of single substrate enzyme catalysed reaction. 23. Explain the main assumption made by Michaelis Menton. 24. Derive Michaelis-Menton equation. 25. What is meant by Michaelis-Menton constant. 26. Give MM-equation and Explain the various terms involved in it. 27. What are the significance of Km and V max.
L] ([Eo] - [ES]) x [ES] [ [ES] - Km 1 + Ki [Eo][ES] - [ES][S] = [ES] [Eo][S] _ ~[S] [ES] lE&J. l Thus uncompetitive inhibition is and In case of uncompetitive inhibitors both Km and Vmax is decreased. The plot of _1_ and -~ which is as shown in the Fig. 16. Vo So Example: An example of un competitive inhibitor is a-KG (a-ketoglutarate) which inhibit the mouse brain. GAB (Gamma amino butyrate) amino transferase which transfers the amino group from y-form to a-form of amino butyrate. -35- Enzymes r + uncompetitive inhibitor Uninhibited ) Fig.
Phosphoramitide Method This method has been developed by Robert Lestrsinger in 1980. In this method more amount of the phosphate is used which allow to under go condensation completely containing the nucleotides. The method can under go condensation upto 150 nucleotide and this is possible when 5'-OH monomer is protected with the same block as earlier DMT. But the reactive 3'end component is the diacetyl phosphoramitide and the product phosphotriester. Structure of phosphoramitide However. this non aqueous reactions sequences adds a single nucleotide to a growing oligonucleotide chain as follows: 1.
College biochemistry. / VI by L Indira; K Nagaraju; Zameer Ahmed K