Michaelis-Menton kinetics, turnover number, unit, specific activity

4 Pages
Unlock Document

Colorado State University
Life Science
LIFE 212
Farida Safadi- Chamberlain

19 September Michaelis-Menton Kinetics Describes irreversible catalytic reactions Km = Michaelis-Menton rate constant (k2+kcat) Km = k1 Reaction rates vary with changes to [substrate] and [enzyme] Fast reaction → smaller Km Enz I Report Plotted A475s [dopachrome, mM] A Calculate C Generate standard curve (y = mx + b) Correlation co-efficient Calc. μmoles dopachrome Dopachrome Plot A475s μmoles mL Used in Enz II lab Enz II Report Part A Calc. Optimum [Enzyme] req. to convert 2 μmoles of DOPA to Dopachrome in 3 to 5 minutes (= 2 mM Dopa) micromoles Calc min Part B Determined pH effects on Velocity (at 1.5 min) A 475vs velocity mM Dopa/micromole Dopachrome μmols Plot velocity ( min ) vs pH Part C Det. Temperature effects on Velocity A 475vs Velocity mM Dopa micromole Dopachrome μmols Plot velocity ( ) vs temperature min μM Velocity is commonly expressed as min Enz III Report 1. Det. A 475 [Product (mM)] & μmols In 0.5 min increments For serial dilution series: 5 different [Substrate] 2. Plot Product (Y axis) vs Minutes (X axis) Put all curves on same graph Calc. slope m = Velocity y2 – y1 (x1, y1) (x2, y2) M = x2−x1
More Less

Related notes for LIFE 212

Log In


Don't have an account?

Join OneClass

Access over 10 million pages of study
documents for 1.3 million courses.

Sign up

Join to view


By registering, I agree to the Terms and Privacy Policies
Already have an account?
Just a few more details

So we can recommend you notes for your school.

Reset Password

Please enter below the email address you registered with and we will send you a link to reset your password.

Add your courses

Get notes from the top students in your class.