Colourmeteric Assay Lab Report

Creatinine is a waste product filtered by the kidneys into the blood (serum) and urine. High serum, and/or urine creatinine levels are indicative of kidney dysfunction. A colorimetric assay can be used to determine the creatinine concentration in the urine and serum samples from patients who are suspected to have kidney dysfunction.

The mole is a convenient unit for analyzing chemical reactions. Avogadro’s number is equal to the mole. The mass of a mole of any compound or element is the mass in grams that corresponds to the molecular formula, also known as the atomic mass. In this experiment, you will observe the reaction of iron nails with a solution of copper (II) chloride and determine the number of moles involved in the reaction. You will determine the number of moles of copper produced in the reaction of iron and copper (II) chloride, determine the number of moles of iron used up in the reaction of iron and copper (II) chloride, determine the ratio of moles of iron to moles of copper, and determine the number of atoms and formula units involved in

The independent variable in this investigation is pH. Each individual enzyme has it’s own pH characteristic. This is because the hydrogen and ionic bonds between –NH2 and –COOH groups of the polypeptides that make up the enzyme, fix the exact arrangement of the active site of an enzyme. It is crucial to be aware of how even small changes in the

It was found that BChE showed broader substrate specificity when compared to AChE, hydrolysing all substrates (at least to some extent), excluding Carbachol. AChE failed to hydrolyse suxamethonium or carbachol to any extent. It was also found that Atropine and Malathion failed to significantly inhibit either cholinesterase, whereas Edrophonium displayed short-acting inhibition. Physostigmine, Nestogmine and Carbachol displayed greater inhibition.

The Uptake of Neutral red dye by saccharomyces cerevisiae in the presence of a metabolic inhibitor

The normalized SDH activity of two homogenates can be compared by looking at the class statistics for the Liver and Kidney homogenate samples in the data sheet attached. The kidney exhibited higher enzyme SDH activity than the liver. This was in agreement with the proposed hypothesis. Comparing the same two homogenates in which malonate was present, it can be seen that the kidney exhibited higher SDH activity than the liver. Thus, both homogenates did in fact have a decrease in enzyme activity, as malonate inhibits the activity of SDH. In successive experiments more malonate was used, and class statistics, not the activity itself, showed lower amounts of enzyme activity/mg protein as reaction number increased and a greater significance. Thus, malonate’s effect did increase proportionally to its concentration. There was a significant difference in SDH activity between the liver and kidney homogenates (p=0.0001)0.05). (Figure 1)

There are two different kinds of inhibitors that affect the activity of enzymes. These two inhibitors are competitive inhibitors and non-competitive inhibitors. Competitive inhibitors act like substrates but instead of causing a reaction it blocks the active site. In order to measure absorption of light, the dye Guaiacol is used. Using the dye is a usefully method for evaluating the activity of enzymes (Doerhe, 1997).

Worthington Biochemical Corporation ha put together many different papers on the effects of enzyme action into one paper. It was originally published in 1972 but was last updated in 2013. This article gives a lot of information on the effects of enzyme action that has been seen on many other articles, it shows to be reliable because of the many authors that have been credited. This is a reliable source because these website holds many other useful experiments and general

- parathesias: a prickly or tingling sensation known as “pins and needles” as a result of pressure or damage to peripheral nerves

Within chemistry exists a branch that studies specifically the rate of chemical reactions. This branch is known as kinetics. The rate at which a chemical reaction occurs is dependent on a variety of factors, including the concentration of reactants present and the temperature, just to name a few. The relationship between the rate at which a reaction occurs and the initial concentration of reactants can be demonstrated through the rate law equation: rate=k〖[A]〗^m 〖[B]〗^n

The Km data from table 4 suggests that a buffer of 7.2 has the highest affinity of ADH to the substrate, ethanol. This experimental data does not correlate with what was found in the literature in either values or trends of

Sampling: Combine 450 uL of 0.15M NaCl, 20 mM Tris-HCL, pH 8, 500 uL of Azocasein, and 50 uL Trypsin into a micro centrifuge tube. We had six samples, three separate pH's were used, one for each of the control tubes with a consistency of three experimental replicates were used to Help with data variation. We allowed the samples to stay in the incubate for 10 minutes. The controls were used to show whether the substrate azocasein would hydrolyze without the enzyme present. We Use the Negative Controls and measured their absorbance because we need to see if the absence of the enzyme would affect the substrate and with an absorbance close to zero. we measured negative with reaction

BglA was remain active even in the existence of 600 mM glucose. However, BglA activity was gradually repressed with the increase of glucose concentration, and Ki value for glucose was found to be 1200 mM as shown in figure 4b. Organic solvents have proven an obvious constrain for the BglA activity, enzyme was completely inactive by adding 40% (v/v) methanol, ethanol, n-butanol and isopropanol whereas, 40% (v/v) acetone, ethyl acetate and acetonitrile strongly repressed BglA activity up to 18%, 38%, 50%, respectively.

In the course of the experiment, the body weight of rats was measured every 7 days. After sacrifice, the lung index was expressed as the ratio of wet lung weight to body weight (g).

For the determination of the kind of inhibition and the enzyme-inhibitor dissociation constant (Ki), the substrate concentration was varied: 0.25, 0.50, 0.75 and 1.0 mmol/L while the inhibitor (5, 6 DHT) was kept at constant concentration for each experiment: 140, 280, 420 or 560 µmol/L.