Lactic Acid Lab Report

Enzymes are types of proteins that work as a substance to help speed up a chemical reaction (Madar & Windelspecht, 104). There are three factors that help enzyme activity increase in speed. The three factors that speed up the activity of enzymes are concentration, an increase in temperature, and a preferred pH environment. Whether or not the reaction continues to move forward is not up to the enzyme, instead the reaction is dependent on a reaction’s free energy. These enzymatic reactions have reactants referred to as substrates. Enzymes do much more than create substrates; enzymes actually work with the substrate in a reaction (Madar &Windelspecht, 106). For reactions in a cell it is

4. Why does potassium concentration rise in patients with acidosis? What is this called? What effects does it have?

In order to generate a bicyclic lactone in this experiment, a Diels-Alder adduct was produced. The bicyclic lactone to be generated was cis-1,3,3a,4,5,7a-Hexahydro-5-methyl-3-oxo-4-isobenzofuran-carboxylic Acid and was produced using a Diels-Alder reaction. The product was also analyzed quantitatively using percent yield. To prepare the Diels-Alder adduct 0.40 g of 2,4-hexadien-1-ol was added to a flask, then 5.00 mL of toluene and 0.40 g of maleic anhydride were added to the flask in that order. The mixture was warmed and stirred to induce a reaction. The reaction progress was monitored using a TLC plate with 30:70 hexane used as the mobile phase and silica gel as the stationary phase. The TLC plate revealed a new spot for the crude product, indicating the reaction had begun.

Hydrochloric acid is produced in the stomach, consisting of chloride and hydrogen. Carbonic acid is produced in red blood cells consisting of carbon dioxide and water, of which is why demanding

Lactose is a sugar that can be put into smaller molecules, glucose and galactose. Lactose is when you are not able to digest milk and dairy meaning that the enzyme lactase that breaks down lactose is not functioning properly. ONPG was used as a substitute for lactase because even though it is colorless it helps show enzyme activity by turning yellow. This experiment measured the absorbance ONPG when exposed to lactase within an environment of different salinity’s. The enzyme, lactase, was obtained by crushing a lactaid pill and then was added into four cuvettes. ONPG and salt solution of different concentrations were added and their levels of absorption was measured by a spectrophotometer. The results showed that higher salt concentrations have a lower level of absorption. There were 4 cuvettes and within those cuvettes that solutions within them were being tested and the results showed the more salt solution added with the lactase the lower the absorbance. The less salt solution there was a higher rate of absorbance. The data supported the hypothesis that with increasing NaCl concentration there would be a decrease in enzyme activity.

When using different methods to measure pH levels there are some tools that can be useful. Some more than others but by putting into action the different methods it may determine which tools will work best and give the best results when testing the pH within a solution. The pH, which stands for the proportion of hydrogen ions in a solution, could be acidic (acidosis), neutral or basic (alkaline). The pH scale goes from numbers 1 through 14. A pH of 7 is neutral;

An increase in calcium inside muscle cells activates processes that generate heat and production of excess acid, leading to a continual increase in body temperature and then acidosis.

An Enzyme is a protein that in essence speeds up biological reactions. So that would mean that a Catalase is an enzyme reaction that decomposes hydrogen peroxide to water and oxygen. It is primarily found in the liver and it is important in protecting the cell from damaging oxidative reactions.

“Enzymes are proteins that have catalytic functions” [1], “that speed up or slow down reactions”[2], “indispensable to maintenance and activity of life”[1]. They are each very specific, and will only work when a particular substrate fits in their active site. An active site is “a region on the surface of an enzyme where the substrate binds, and where the reaction occurs”[2].

How does the blood pH value change as Pco2 changes? The Pco2 binds with the water in the blood to form carbonic acid which then forms H+ and HCO3-. When the H+ increases it causes the blood to become more acidic and lowers the pH, and when the H+ is low the blood pH rises.

One of the basic concepts that new nurses need to learn is that homeostasis in the body is maintained by the acid base balance in the body. That concept is critical when looking at arterial blood gases. This can help guide the nurse to anticipate what the doctor will order and the education that she needs to give the patient and the family. This case study should help to illustrate the point.

CAUSES — The causes of lactic acidosis can generally be divided into those associated with obviously impaired tissue oxygenation (type A) and those in which systemic impairment in oxygenation does not exist or is not readily apparent (type B) (table 1). However, in reality, there is frequently overlap between type A and type B lactic acidosis. In sepsis, for example, there is both an increase in lactate production resulting from microcirculatory failure and also a decrease in lactate clearance that is not solely due to diminished oxygen

The second type is called heterolactic fermentation and produces lactate as well as carbon dioxide and acids. Lactate dehydrogenase is involved in homolactic fermentation (). Both forms of lactic acid fermentation use the Embden-Myerfhof glycolytic pathway to convert the carbohydrate glucose into ATP, NADH, and pyruvate (). The formation

Isoenzymes of Lactate Dehydrogenase (LDH) Part A: Separating Lactate Dehydrogenase (LDH) isoenzymes from tissue homogenates using electrophoresis Introduction Isoenzymes of Lactate Dehydrogenase (LDH) in plasma are used to indicate whether a person has suffered a recent heart attack or is suspected to have liver disease. LDH is found in both plants and animals, it is an enzyme that catalyses the conversion of pyruvate and lactate. Pyruvate is the final product of glycolysis, in glycolysis energy in the form of Adenosine Triphosphate (ATP) is produced from glucose. Isoenzymes are variant forms of the same enzyme that occur within an individual, the variants can have slight differences in amino acid sequence, in catalytic activity and also differ in their occurrence in particular tissues.

Metabolic acidosis results from all conditions that decrease the pH of the body fluids below 7.35 and HCO3- levels are <22 mEq/L, with the exception of conditions resulting from altered function of the respiratory system. As hydrogen ions accumulate in the body fluids, buffers first resist a decline in pH. If the buffers cannot compensate for the increase in hydrogen ions, the respiratory center helps regulate the body fluid pH. The reduced pH stimulates the respiratory center, which causes hyperventilation. During hyperventilation, carbon dioxide is eliminated at a greater rate. The elimination of carbon dioxide also eliminates excess hydrogen ions and helps maintain the pH of the body fluids within a normal range. (Angus, 2006)