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This is complemented by gastro-coronary reflexes [12] whereby the coronary arteries constrict with "functional cardiovascular symptoms" similar to chest-pain on the left side and radiation to the left shoulder, dyspnea, sweating, up to angina pectoris-like attacks with extrasystoles, drop of blood pressure, and tachycardia (high heart rate) or ...
Pepsin / ˈ p ɛ p s ɪ n / is an endopeptidase that breaks down proteins into smaller peptides and amino acids. It is one of the main digestive enzymes in the digestive systems of humans and many other animals, where it helps digest the proteins in food. Pepsin is an aspartic protease, using a catalytic aspartate in its active site. [2]
Carboxypeptidase A and the target enzyme of Captopril, angiotensin-converting enzyme, have very similar structures, as they both contain a zinc ion within the active site. This allowed for a potent carboxypeptidase A inhibitor to be used to inhibit the enzyme and, thus, lower blood pressure through the renin-angiotensin-aldosterone system. [1]
Bicarbonate is a base that neutralizes the acid, thus establishing a pH favorable to the action of other digestive enzymes in the small intestine. [ 26 ] Secretin also increases water and bicarbonate secretion from duodenal Brunner's glands to buffer the incoming protons of the acidic chyme, [ 24 ] and also reduces acid secretion by parietal ...
[6] [7] [8] VIP stimulates contractility in the heart, causes vasodilation, increases glycogenolysis, lowers arterial blood pressure and relaxes the smooth muscle of trachea, stomach and gallbladder. In humans, the vasoactive intestinal peptide is encoded by the VIP gene. [9] VIP has a half-life (t ½) in the blood of about two minutes. [10]
Some, but not all, carboxypeptidases are initially produced in an inactive form; this precursor form is referred to as a procarboxypeptidase. In the case of pancreatic carboxypeptidase A, the inactive zymogen form - pro-carboxypeptidase A - is converted to its active form - carboxypeptidase A - by the enzyme trypsin. This mechanism ensures that ...
Chief cells are part of fundic gland polyps (here shown in high magnification). [11]In gastric tissue, a loss of parietal cells due to chronic inflammation has been shown to affect chief cell differentiation and can induce chief cells to transdifferentiate back into neck cells and can lead to the formation of mucus cell metaplasia known as spasmolytic polypeptide expressing metaplasia (SPEM ...
PEPCK (EC 4.1.1.49) is one of three decarboxylation enzymes used in the inorganic carbon concentrating mechanisms of C 4 and CAM plants. The others are NADP-malic enzyme and NAD-malic enzyme. [17] [18] In C 4 carbon fixation, carbon dioxide is first fixed by combination with phosphoenolpyruvate to form oxaloacetate in the mesophyll.