Kinetic Properties Of Wheat Germ Aldolase

Kinetic Properties of Wheat Germ Phosphatase Results: 1. The final concentration of astringent Phosphatase enzyme in this reaction was 0.07 ìM, the final inhibitor concentration was 0.67 ìM. (see sample tally unitary). 2. tabular array 1. Enzyme-Substrate answer (Un stamp down) render         Concentration of PNPP (mM)          mountain of 5.0mM PNPP (ml)         Volume of dH2O (ml)         A405          hurrying*(ìbulwark/min) 1         0         0         4.3         0 (blank)         0 2         0.05         0.05         4.25         0.148         0.0118 3         0.075         0.075         4.225         0.199         0.0159 4         0.113         0.113         4.187         0.231         0.0184 5         0.170         0.170         4.130         0.286         0.0228 6         0.255         0.255         4.045         0.337         0.0269 7         0.384         0.384         3.916         0.398         0.0318 8         0.578         0.578         3.722         0.414         0.0330 9         0.88         0.88         3.42         0.507         0.0405 10         1.32         1.32         2.98         0.578         0.0461 11         2.0         2.0         2.3         0.655          0.0523 12         3.0 !         3.0         1.3         0.708         0.0565 7         0.384         0.384         3.916         0.324         0.0259 * See Sample Calculation #2. 7 is a send of tube #7. 3. control panel 2. Enzyme-Substrate Reaction (Inhibited) Tube         Concentration of PNPP (mM)         Volume of 5.0mM PNPP (ml)         Volume of 1.5mM K2HPO4 (ml)         Volume of dH20 (ml)         A405         Velocity(ìmol/min) 1         0         0         1         3.3         0 (blank)         0 2         0.05         0.05         1         3.25         0.002         0.0002 3         0.075         0.075         Â 1         3.225         0.002         0.0002 4         0.11         0.11         1         3.19         0.023         0.0018 5         0.17         0.17         1         3.13         0.070         0.0056 6         0.26         0.26         1         3.04         0.081         0.0065 7         0.38         0.38         1         2.91         0.103         0.0082 8         0.58         0.58         1         2.72         0.116         0.0093 9         0.88         0.88         1         2.42          0.161         0.0128 10    Â!  Â Â Â Â 1.32         1.32         1         1.98         0.226         0.0180 11         2.00         2.00         1         1.3         0.302         0.0241 12         3.00         3.00         1         0.3         0.418         0.0334 3. Graph one 4. Graph two 5. Table 3: Km and Vmax value Plot type         Km uninhibited         Km inhibited         Vmax uninhibited         Vmax inhibited MM*         0.28         4.00         0.72         0.95 LB         0.15         31.09         0.047         0.62 * See committed Kinetic printouts. Sample Calculations 1.         Enzyme: V1M1 = V 2M2 (0.2ml)(2.5ìM Acid Phosphatase) = (7.5ml)(M2) M2 = 0.07 ìM Inhibitor: V1M1 = V2M2 (1ml)(5mM K2HPO4) = (7.5ml)(M2) M2 = 0.67 ìM 2. Velocity (aka. Enzyme Activity) Example: Tube 2 of Uninhibited a.          practice absorbance to find concentration. c = A/(Ã¥l) = (0.148)/[(18.8x103L/mol-cm)(1cm)] = 7.87 x... If you want to get a full essay, order it on our website: BestEssayCheap.com

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