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The process of fibrinolysis disposes of bacteria when healing has occurred?
Fibrinolysis is the process of breaking down blood clots by the enzyme plasmin. While fibrinolysis does not directly dispose of bacteria, it plays a role in the immune response by assisting in the removal of debris and pathogens from the site of injury once healing has occurred.
Which antigen is being destroyed by proteolytic enzyme treatment of red cells?
Proteolytic enzyme treatment of red cells destroys A and B antigens, which are present on the surface of red blood cells. This process is often used to convert group AB red cells into group O red cells for safe transfusion to patients with severe blood type mismatches.
What is the next step in the process after a substrate enters the active site of an enzyme?
After a substrate enters the active site of an enzyme, it undergoes a conformational change to fit the substrate more closely. This induces a chemical reaction to occur, resulting in the formation of the enzyme-substrate complex.
Which enzyme binds to DNA during transcription?
RNA polymerase is the enzyme that binds to DNA during transcription.
In the stomach the protein is digested by?
Protein digestion in the stomach is initiated by the enzyme pepsin, which breaks down proteins into smaller peptides. Pepsin is activated by the acidic environment of the stomach, specifically hydrochloric acid. The breakdown of proteins into peptides is essential for their absorption and utilization by the body.
What clot buster enzyme removes unneeded clots after healing has occurred during fibrinolysis?
plasmin
What is least likely to be a mechanism for enzyme regulation?
Change in enzyme concentration through gene expression.
The process of fibrinolysis disposes of bacteria when healing has occurred?
Fibrinolysis is the process of breaking down blood clots by the enzyme plasmin. While fibrinolysis does not directly dispose of bacteria, it plays a role in the immune response by assisting in the removal of debris and pathogens from the site of injury once healing has occurred.
Location and function of pepsin?
pepsin is a proteolytic enzyme present in the gastric glands.it hydrolyses proteins into peptones.
Does proteolytic enzymes cause denature of proteins?
Yes, proteolytic enzymes break down proteins by cleaving peptide bonds. This process may result in protein denaturation, especially if the enzyme cleaves at specific sites that disrupt the protein's structure and function.
What is a vasodilator that can be inactivated by a proteolytic enzyme?
Nitric oxide is a vasodilator that can be inactivated by proteolytic enzymes such as superoxide dismutase or hemoglobin. These enzymes can break down nitric oxide, reducing its vasodilatory effects.
Which antigen is being destroyed by proteolytic enzyme treatment of red cells?
Proteolytic enzyme treatment of red cells destroys A and B antigens, which are present on the surface of red blood cells. This process is often used to convert group AB red cells into group O red cells for safe transfusion to patients with severe blood type mismatches.
What is dissolving of a thrombus called?
The dissolving of a thrombus is called fibrinolysis. This process involves breaking down the fibrin mesh that holds the clot together, usually through the action of the enzyme plasmin.
What is the next step in the process after a substrate enters the active site of an enzyme?
After a substrate enters the active site of an enzyme, it undergoes a conformational change to fit the substrate more closely. This induces a chemical reaction to occur, resulting in the formation of the enzyme-substrate complex.
What happens to an enzyme when it is destroyed?
When an enzyme is destroyed, its structure is altered by factors such as high temperature or extreme pH, resulting in loss of its catalytic activity. Once destroyed, an enzyme cannot perform its biological function, leading to impaired biochemical reactions in the cell or organism. The destroyed enzyme is typically broken down into its component amino acids by proteolytic enzymes in the body.
What is allosteric activator?
An allosteric activator is a molecule that binds to a specific site on an enzyme, distinct from the active site, and enhances the enzyme's activity. This binding induces a conformational change in the enzyme, leading to an increase in its catalytic activity. Allosteric activators are essential for regulating enzyme activity in various cellular processes.
What is the gastric enzyme that acts on proteins?
The proteolytic or protein eating enzyme of the stomach is called pepsin. Pepsin is secreted into the stomach as a zymogen (or inactive enzyme precursor) called pepsinogen which is converted into the active enzyme form by the hydrochloric acid and low pH in the gastric juices.
