Ascp High Yield Clinical Chemistry Terms From Michael Bishop Book!

Amylase is the enzyme responsible for breaking down starch and glycogen, specifically targeting the 1-6 branching linkages. Lipase, Protease, and Cellulase are enzymes that are involved in the breakdown of lipids, proteins, and cellulose respectively.

Amylase is an enzyme that helps in the digestion of carbohydrates. Increased levels of amylase in the blood are often associated with acute pancreatitis, which is inflammation of the pancreas. This condition can cause amylase levels to rise significantly.

The correct term for measuring color in this context is 'chromogenic', which refers to the production of color by a chemical reaction.

Continuous monitoring of amylase activity involves constantly measuring the enzyme system over a period of time to track any changes or fluctuations in activity. This method provides a more consistent and accurate representation of the enzyme's behavior compared to periodic, one-time, or random monitoring.

Amylopsin is another name for Pancreatic Amylase which is a digestive enzyme produced by the pancreas to help break down carbohydrates into sugars. Lipase, Trypsin, and Pepsin are other digestive enzymes but are not specific to carbohydrate breakdown.

Lipase is the enzyme responsible for breaking down fats into alcohols and fatty acids through hydrolysis. Amylase acts on carbohydrates, protease acts on proteins, and cellulase acts on cellulose, not fats.

Lipase is a pancreatic enzyme that is elevated in the blood during acute pancreatitis, making it a specific marker for this disease.

In the Tietz and Cherry Crandall methods for determining lipase, the substrate used is typically 50% olive oil or triolein. These fats are broken down by lipase enzymes in the presence of lipase, leading to the release of fatty acids which can be measured as an indicator of lipase activity.

The end point of Tietz and Cherry Crandall methods in determining lipase is when fatty acid or oleic acid is produced as a result of hydrolysis.

Creatine kinase (CK) is an enzyme found in various tissues in the body, with the highest activities typically seen in the CNS (Central Nervous System), Heart, and Skeletal muscle. These tissues have high energy demands and rely on CK for energy metabolism.

The correct term for measuring the disappearance of starch substrate is Amyloclastic, which specifically refers to the breakdown or degradation of starch. The incorrect answers are: Amylopexy (surgical removal of starch), Amylolytic (related to the breakdown of starch by enzyme amylase), and Amylogenesis (the formation or synthesis of starch).

Salivary Amylase is also commonly referred to as Ptyalin.

In the Tietz and Cherry Crandall methods for determining lipase, the correct titrating agent is 0.4 NaOH, as it is commonly used for the alkaline titration process to measure lipase activity levels accurately.

The correct indicator for Tietz method in determining lipase is Thymolphthalein + veronal. This indicator helps in accurately measuring lipase activity in biological samples.

The indicator used in the Cherry Crandall method for determining lipase is Phenolphthalein, which changes color in the presence of lipase activity.

The end color of Tietz method in determining lipase is blue due to the reaction that takes place in the presence of lipase.

GGTP is primarily used as a diagnostic marker for hepatobiliary disorders and chronic alcoholism due to its elevated levels in these conditions.

The Szaz assay specifically measures the enzyme activity of GGTP by detecting the absorbance of p-Nitroaniline at 405-420 nm. The Bradford assay, Lowry assay, and Bicinchoninic Acid assay are commonly used for protein quantification but not for GGTP enzyme activity measurement.

The Cherry Crandall method in determining lipase results in a pink color at the end, indicating the presence of lipase activity.

Acid phosphatase is specifically known for catalyzing the hydrolysis of phosphomonoesters and is used in the mentioned evaluations. Alkaline phosphatase, lipase, and amylase are enzymes that do not perform these specific functions.

L-tartrate ions are known to inhibit specific prostatic acid phosphatase (ACP), while the incorrect answers do not have any inhibitory effect on prostatic ACP.

To calculate prostatic ACP, you need to subtract the ACP after from the Total ACP.

Formaldehyde in combination with cupric ions is known to inhibit red cell ACP activity, while the other incorrect combinations do not have the same inhibitory effect.

Thymolphthalein monophosphate is the specific substrate used in the quantitative end point method of ACP determination. The other options are incorrect substrates with similar names but not utilized in this particular method.

The correct substrate for the continuous monitoring method of ACP determination is a-naphthyl phosphate, as it is specifically designed to react with alkaline phosphatase enzyme to produce a colored product that can be continuously monitored for ACP activity.

The reference range for prostatic ACP is 0-3.5 mg/mL, which is the correct answer. It is important to understand the normal range to assess any deviations in the levels and make informed decisions based on the results.

Continuous monitoring method for ACP determination utilizes a-naphthyl phosphate as the substrate, not b-naphthyl phosphate, c-naphthyl phosphate, or d-naphthyl phosphate.

The reference range for prostatic ACP is 0-3.5 mg/mL, which indicates the normal levels of Acid Phosphatase specifically found in the prostate gland. Values outside of this range may suggest an underlying condition.

CK, also known as creatine kinase, is an enzyme found in muscle cells that helps transfer high-energy phosphate groups from ATP to creatine. This process helps in the rapid production of ATP during short bursts of intense physical activity.