Ams, Lps, ACP And Others

The marker for Wilson's disease is ceruloplasmin. In this question, the correct answer is provided in three different formats: all lowercase (ceruloplasmin), all uppercase (CERULOPLASMIN), and capitalized (Ceruloplasmin). All three formats are acceptable and refer to the same marker for Wilson's disease.

Amylase is an enzyme that converts starch into glucose and maltose. This process is known as amylolysis and occurs in the digestive system. Amylase breaks down the long chains of starch molecules into smaller sugar molecules, such as glucose and maltose, which can be easily absorbed by the body. Therefore, amylase plays a crucial role in the digestion and absorption of carbohydrates in the body.

Calcium acetate and sodium chloride are compounds that serve as activators in serum amylase determination. These compounds enhance the enzymatic activity of serum amylase, allowing for more accurate and efficient determination of its concentration. Sodium azide and potassium thiocyanate, on the other hand, do not serve as activators in this process.

Acid phosphatase is needed in the coupled enzymatic method for ACP determination. This enzyme is responsible for catalyzing the hydrolysis of phosphate groups from organic compounds under acidic conditions. In the coupled enzymatic method, acid phosphatase is used to convert the substrate into a product that can be further detected or quantified using other enzymes. This suggests that acid phosphatase plays a crucial role in the overall enzymatic reaction and is necessary for accurate ACP determination.

The explanation for the given correct answer, "Both statements are true," is that ACE (angiotensin-converting enzyme) levels are indeed elevated in diseases that involve the abnormal collection of inflammatory cells forming granulomas. This is because ACE is produced by these inflammatory cells. Additionally, ACE levels are increased in Hansen's disease, also known as leprosy. Therefore, both statements accurately reflect the role of ACE in diseases involving granulomas and Hansen's disease.

The first statement is true because acute pancreatitis is known to cause an increase in the serum levels of AMS (acute phase reactants) and LPS (lipopolysaccharides). However, the second statement is false because the elevated levels of AMS actually persist for a shorter duration compared to LPS in this disease.

The first statement is false because AMS is not involved in lipid metabolism, but rather in the synthesis of adenosine monophosphate (AMP). The second statement is true because LPS, also known as glycogen phosphorylase, is involved in the breakdown of starch and glycogen. Therefore, the correct answer is that the first statement is false and the second statement is true.

The given answer states that both statements are true. According to the information provided, 5'NT, GGT, AST, and LDH are elevated in liver and hepatobiliary diseases, indicating that the first statement is true. On the other hand, AMS and LPS are primarily located in the pancreas, suggesting that the second statement is also true. Therefore, the correct answer is that both statements are true.

LPS (lipopolysaccharide) is the most specific enzyme for acute pancreatitis. LPS is a component of the outer membrane of certain bacteria, and its presence in the bloodstream is a marker of bacterial infection. In acute pancreatitis, LPS can enter the bloodstream due to inflammation and damage to the pancreas. Therefore, elevated levels of LPS can indicate the presence of acute pancreatitis. ACP (acid phosphatase), AMS (amylase), and LDH (lactate dehydrogenase) are enzymes that can also be elevated in acute pancreatitis, but they are not as specific to this condition as LPS.

Macroamylasemia is a condition characterized by the presence of high levels of amylase in the blood, while the levels of amylase in the urine remain within the normal range. Therefore, the answer "increased serum AMS and normal urine AMS" is consistent with macroamylasemia.

The correct answer is "Amyloclastic" because it is a method for AMS determination that follows the 1st order enzymatic reaction. This method involves the enzymatic breakdown of amylose, a component of starch, into smaller fragments. The rate of this enzymatic reaction can be measured to determine the concentration of AMS (amylose) present in a sample. Other options like "Saccharogenic" and "Chromogenic" do not specifically mention the enzymatic breakdown of amylose, while "Coupled enzymatic method" is a more general term that does not specifically indicate the 1st order enzymatic reaction for AMS determination.

The best enzyme substrate for continuous monitoring method for ACP is alpha-naphthyl-phosphate. This substrate is preferred because it produces a continuous color change when acted upon by ACP, allowing for easy and continuous monitoring of the enzyme activity. Phenyl-phosphate, thymolphthalein monophosphate, and beta-glycerophosphate may also be substrates for ACP, but they do not provide the same continuous color change, making them less suitable for continuous monitoring.

The given statements are all true except for the statement that LPS is associated with the Hexokinase coupling method. The other statements correctly associate 5'NT with Dixon and Purdon, CHS with the Ellman technique, and ACP with Roy and Hillman. However, there is no known association between LPS and the Hexokinase coupling method.

ACP, or acid phosphatase, is an enzyme that is found in high concentrations in seminal fluid. Therefore, testing for the presence of ACP can help establish the presence of seminal fluid. LDH, ALP, and ICD are not specific markers for seminal fluid and would not provide reliable evidence of its presence.

The Tietz and Fiereck method is used in the laboratory experiment for LPS determination. This method involves the use of peroxidase coupling to detect and measure the presence of LPS. It is a reliable and widely used technique for quantifying LPS levels in samples. The method is based on the principle of enzymatic reactions and utilizes specific reagents to generate a colorimetric signal that is proportional to the LPS concentration. This allows for accurate and precise measurement of LPS levels in various biological samples.

In colorimetric methods for AMS determination, CNP (p-nitrophenyl phosphate) is the end product that is directly measured to estimate enzyme activity. CNP is a substrate that is cleaved by the enzyme being studied, resulting in the release of p-nitrophenol. The amount of p-nitrophenol produced is directly proportional to the enzyme activity, and it can be measured by its absorbance at a specific wavelength. Therefore, CNP is the correct answer as it is the end product that is directly measured in this method.

The given answer is correct because it states that both statements are true. The first statement is true because cholinesterase can indeed be used as a marker for organophosphate poisoning. Organophosphates inhibit the activity of cholinesterase enzyme, leading to its decreased levels in the body. The second statement is also true because low cholinesterase levels in the sweat can validate insecticide/pesticide poisoning, as these substances often contain organophosphates. Therefore, both statements are accurate.

The explanation for the given correct answer is that the first statement is true because macroamylasemia is indeed an asymptomatic condition resulting from the combination of AMS molecule and immunoglobulin to form a complex. However, the second statement is false because the complex formed is actually too large to be retained by the glomerulus, leading to increased AMS levels in the serum.

The explanation for the given correct answer is that the Cherry Crandal method does involve the lipolytic action of lipase in the serum to hydrolyze the olive oil emulsion. This process leads to the formation of fatty acids and alcohol. However, the decrease in turbidity is not proportional to the lipase activity in the serum. Therefore, the first statement is true and the second statement is false.

The substrate used in the colorimetric method for ACP determination is p-nitrophenolphosphate. This substrate produces p-nitrophenol as the end product. It can also be referred to as P-NITROPHENOLPHOSPHATE or PNPP.