Bio-E1a-2011-Outline

Bio-E1a-2011-Outline - Bio E1a Outline of Lab Material for...

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Bio E1a – Outline of Lab Material for Lab Practical Review For Lab Review and Practical we are having back to back times scheduled for both nights for all sections. Each lab section is in its normal room but only at a specific time, as follows: Section Normal Day: Review: Practical: Mondays Wed., Dec 7, 7:35 - 8:30pm Mon., Dec 12, 8:35 - 9:30pm Wednesdays Wed., Dec 7, 8:35 - 9:30pm Mon., Dec 12, 7:35 - 8:30pm Practical Test Format: c. 25 Questions/Stations in a room (most require 2 or 3 short answers on your answer sheet). Value: 100 Points. Timed: 1.5 minutes/Question. 3 min at end for finishing calculations. Please Bring A Calculator To The Practical. Know how to do all types of calculations you did during this summer in lab. Formulae will be provided. Know what every bold or italic term in every lab protocol means. I) Enzymes A) Competitive Inhibition 1) Inhibitor similar in shape and charge to substrate of enzyme a) Binds to Active Site taking time away from enzyme substrate reaction reducing product production rate (E=Enzyme, S= Substrate, P=Product, I=Inhibitor): E + I < -> EI complex, the inhibition competes with E + S -> ES complex -> E + P , the normal enzymatic reaction. b) Adding extra substrate to system with competitive inhibitor increases the enzyme rate proportional to ratio of substrate to inhibitor. Non-competitive inhibitors do not show increased rate with extra substrate. 2) Succinic Dehydrogenase from calf heart muscle mitochondria a) Substrate: Succinic Acid, Product: Fumaric Acid, Coupled to FAD reduction to FADH 2 b) Inhibitor: Malonic acid (binds and unbinds to Succinic Dehydrogenase) c) Indicator: Methylene Blue, turns clear with reduction (in place of FAD reduction) B) Enzyme Concentration and pH Effects: 1) α -Amylase from pig pancreas (identical to Salivary α -Amylase) a) Substrate: Starch, Product: Maltose b) Indicator: IKI Starch Test (Iodine + Potassium Iodide) turns blue when starch is present but remains yellow when reaction is complete. c) Rate is calculated as quantity of substrate reacted/time. 2) Concentration Effect: increasing α -Amylase concentration increases rate nearly linearly. 3) pH Effect: Enzymes have an optimum pH where the highest rate is found. At non-optimum pH levels the enzyme may be partially or wholly denatured reducing or destroying rate by effecting the active site’s shape and charges. a) α -Amylase has peak rate at slightly more alkaline than pH 7.0. Other enzymes may have very different optima.
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II) Photosynthesis, Light Absorption and the Light Reactions A) Absorption Spectrum 2) Isolating Spinach Chloroplasts a) Isolated from homogenized leaves using Differential Centrifugation i) First spin is slow and pellets large particles and cell debris, leaving less dense organelles in supernatant. ii) Second spin is fast and pellets the chloroplasts, leaving less dense substances in the supernatant.
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This note was uploaded on 02/09/2012 for the course BIOLOGY 102 taught by Professor Anderson during the Spring '11 term at Harvard.

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Bio-E1a-2011-Outline - Bio E1a Outline of Lab Material for...

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