Plasmin is an important enzyme (EC 3.4.21.7) present in blood that degrades many blood plasma proteins, including fibrin clots. The degradation of fibrin is termed fibrinolysis. In humans, the plasmin protein is encoded by the PLG gene.[5]
https://en.wikipedia.org/wiki/Plasmin
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Renin (etymology and pronunciation), also known as an angiotensinogenase, is an aspartic protease protein and enzyme secreted by the kidneys that participates in the body's renin–angiotensin–aldosterone system (RAAS)—also known as the renin–angiotensin–aldosterone axis—that mediates the volume of extracellular fluid (blood plasma, lymph and interstitial fluid) and arterial vasoconstriction. Thus, it regulates the body's mean arterial blood pressure.
Renin is not commonly referred to as a hormone, albeit it having a receptor, the (pro)renin receptor, also known as the renin receptor and prorenin receptor (see also below),[4] as well as enzymatic activity with which it hydrolyzes angiotensinogen to angiotensin I.
https://en.wikipedia.org/wiki/Renin
The carbonic anhydrases (or carbonate dehydratases) form a family of enzymesthat catalyze the interconversion between carbon dioxide and water and the dissociated ions of carbonic acid (i.e. bicarbonate and hydrogen ions).[1] The active site of most carbonic anhydrases contains a zinc ion. They are therefore classified as metalloenzymes. The enzyme maintains acid-base balance and helps transport carbon dioxide.[2]
Carbonic anhydrase helps maintain acid–base homeostasis, regulate pH, and fluid balance. Depending on its location, the role of the enzyme changes slightly. For example, carbonic anhydrase produces acid in the stomach lining. In the kidney, the control of bicarbonate ions influences the water content of the cell. The control of bicarbonate ions also influences the water content in the eyes. Inhibitors of carbonic anhydrase are used to treat glaucoma, the excessive build up of water in the eyes. Blocking this enzyme shifts the fluid balance in the eyes of the patient to reduce fluid build up thereby relieving pressure.[2][3]
The Bohr Effect is a way to describe hemoglobin's oxygen binding affinity. The Bohr Effect was described by Christian Bohr in the year 1904, and it refers to a shift in an oxygen dissociation curve that is caused by a change in concentration of carbon dioxide or a change in the pH. Essentially an increase in carbon dioxide results in lowered blood pH which lowers oxygen-hemoglobin binding.[4] The opposite is true where a decrease in the concentration of carbon dioxide raises the blood pH which raises the rate of oxygen-hemoglobin binding. Relating the Bohr Effect to carbonic anhydrase is simple: carbonic anhydrase speeds up the reaction of carbon dioxide reacting with water to produce hydrogen ions (protons) and bicarbonate ions.
To describe equilibrium in the carbonic anhydrase reaction, Le Chatelier's principle is used. The tissues are more acidic than the lungs because carbon dioxide is produced by cellular respiration and it reacts with water in the tissues to produce the hydrogen protons. Because the carbon dioxide concentration is higher, equilibrium shifts to the right, to the bicarbonate side. The opposite is seen in the lungs where carbon dioxide is being released so its concentration is lower so equilibrium shifts to the left towards carbon dioxide to try and raise its concentration.[5]
https://en.wikipedia.org/wiki/Carbonic_anhydrase
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