Determination of an Unknown Amino Acid from Titration

8 test tubes were then labelled A-H, 1ml of DCPIP was added to each of the test tubes. 2ml of NaHCO3 was added tubes A through G.

Purpose: To become familiar with the International System of Units and common laboratory equipment and techniques. To learn how to determine volume, mass, length, and temperature of a wide variety of items. To learn how to calculate density and concentration of dilutions.

First I will set up the apparatus as show above. I will add 1.5 grams

By extrapolating from the curve, the concentration of the unknown solution is ≈ 1.9mg.mL. The rate of reaction increases linearly with an increase in the substrate concentration.

This amount was then weighed to be 0.060 g, 21.74% (see figure 2) of the total mass of Panacetin. According to the label, the sucrose should make up about 10% of the composition, thus this sample weighed about 11.74% percent more than expected. This increase of weight may of been caused by many different experimental errors, such as the failure to isolate the solid completely after centrifugation. When extracting the pellet from the bottom of the tube, it is possible that some of the dissolved liquid was collected to, yielding a larger mass.

* By using the dropper and measuring cylinder, 3ml of 1% lipase was added into the test tube

0.1 gram of my product from the second trial was weighed in a tray and was then added to a fourth test tube containing 2.0 mL of Iron (III) chloride, which was measured using a 10 mL graduated cylinder, to test for

The purpose of this experiment was to determine the pKa, Ka, and molar mass of an unknown acid (#14). The pKa was found to be 3.88, the Ka was found to be 1.318 x 10 -4, and the molar mass was found to be 171.9 g/mol.

The purpose of this lab was to become familiar with the three different balances and two different methods used to find the weight and mass of chemicals and compounds in the ChemLab program. The lab was performed by using three different types of balances, and the direct weighing and weighing by difference methods.

Determine the weight of the water by subtracting the weight of the vial with water by the weight of the vial on its own.

A total of 1.5 mL was added to produce a pH of around 6. The mixture was stirred for an additional 30 minutes.

One milliliter of 6.00-M phosphoric acid was placed into a 125-mL Erlenmeyer flask using a volumetric pipette. Using a slightly larger pipette, six milliliters of 3.00-M sodium hydroxide was transferred into a 50-mL beaker. Then a disposable pipette was used to slowly mix the sodium hydroxide into the phosphoric acid while the solution was swirled around. Then both the beaker and flask were rinsed with 2-mL of deionized water and set aside. A clean and dry evaporating dish was weighed with watch glass on a scale. Then the solution was poured into the dish and the watch glass was placed on top. The solution was then heated with a Bunsen burner to allow for the water to boil off to reveal a dry white solid. After the dish cooled to room temperature it was once again weighed and the new mass was recorded.

Aminotransferases are enzymes involved in catalyzing reactions between amino acid and α-keto acid. Amino acid such as L-glutamate contains an amine group whereas α-keto acid such as pyruvate contains a keto group. The amine group of L-glutamate is exchanged with the keto group of α-keto acid resulting in the α-keto acid becoming an amino acid and the amino acid becoming a keto acid. Aminotransferase catalyzes the reaction of transferring α-amino group of L-glutamate to pyruvate in exchange for the α-keto group of pyruvate where L-alanine and α-ketoglutarate are formed. Aminotransferases are specific for the amino acid formed and reactions catalyzed by aminotransferases are reversible. Aminotransferase used in the formation of alanine is called glutamate-pyruvate aminotransferase (GPT) where in the formation of aspartate, glutamate-oxaloacetate aminotransferase (GOT) is used. (Vroon, D., & Israili, Z, 1990)

First of all, from the sense strand given in the question, I derived the antisense strand for it. This is done by using the complementary Nitrogenous base concept. Guanine complements Cytosine, Thymine complements Adenine and vice versa. Once this is done, we obtain the antisense strand.

Identifying amino acids and quantifying protein are common yet important experiments performed in the field of biochemistry, with each having multiple ways to execute the experiment. In determining the identity of an unknown amino acid, an acid base titration was chosen and can be utilized by way of creating a titration curve. This allows for the determination of pH, which can be used to identify different groups on an amino acid and distinguish the correct amino acid. Due to amino acids being amphoteric with a basic amino group, an acidic carboxyl group, and sometimes an acidic or basic side chain, two titrations were performed with one using hydrochloric acid (HCl) as the acidic titrant and the other using potassium hydroxide (KOH) as a basic titrant. By observing the titration curve, the experimentally obtained equivalence points can then be used to compare against literature values of amino