Enzyme Kinetics Lab - Enzyme Kinetics of β-Galactosidase...

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Enzyme Kinetics of β -Galactosidase Measure product formation Analyze data Michaelis-Menten Lineweaver-Burk Tells us it’s an enzyme (usually)
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Enzymes Protein catalysts Speed up chemical reactions without changing the equilibrium Increase reaction rate by decreasing E a Substrate binds at the active site thru H-bonds, electrostatic interactions, etc.
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Enzyme Kinetics Provide specific information about an enzyme Velocity (V) is the measure of the rate of catalysis V increases as [S] increases BUT only to a certain point (saturation) 2 important terms in enzyme kinetics V max : maximum velocity; enzyme saturation/all active sites are occupied K m : indicates strength of binding of the substrate to the active site; Km = [S] at ½ V max Lower K m indicates increased strength of binding
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Michaelis-Menten Equation Allows us to relate K m and V max V=(V max *[S])/([S]+ K m ) [M-M curve] 1/v = (K m /V max )1/[s] + 1/V max [L-B] M-M [S] v L-B 1/[S] 1/v Difficult to evaluate K m therefore, linearize M-M equation
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This lab report was uploaded on 04/08/2008 for the course BIOL 301 taught by Professor Tepperman during the Winter '08 term at University of Cincinnati.

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Enzyme Kinetics Lab - Enzyme Kinetics of β-Galactosidase...

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