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pepsin
en
(biochemistry) A digestive enzyme that chemically digests, or breaks down, proteins into shorter chains of amino acids.
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Under non-acid conditions (neutral pH), pepsin is internalized by cells of the upper airways such as the larynx and hypopharynx by a process known as receptor-mediated endocytosis.
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Hydrochloric acid creates an acidic environment, which allows pepsinogen to unfold and cleave itself in an autocatalytic fashion, thereby generating pepsin (the active form).
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An acidic substance that was able to convert nitrogen-based foods into water-soluble material was determined to be pepsin.
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Pepsin exhibits maximal activity at pH 2.0 and is inactive at pH 6.5 and above, however pepsin is not fully denatured or irreversibly inactivated until pH 8.0.
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In humans and many other animals, hydrochloric acid is a part of the gastric acid secreted within the stomach to help hydrolyze proteins and polysaccharides, as well as converting the inactive pro-enzyme, pepsinogen into the enzyme, pepsin.
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The statyl residue of pepstatin is thought to be responsible for pepstatin inhibition of pepsin; statine is a potential analog of the transition state for catalysis by pepsin and other acid proteases.
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Pepsin is commonly used in the preparation of F(ab')2 fragments from antibodies.
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The conclusion that pure proteins can be enzymes was definitively proved by Northrop and Stanley, who worked on the digestive enzymes pepsin (1930), trypsin and chymotrypsin.
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Pepsin is used for a variety of applications in food manufacturing: to modify and provide whipping qualities to soy protein and gelatin, to modify vegetable proteins for use in nondairy snack items, to make precooked cereals into instant hot cereals, and to prepare animal and vegetable protein hydrolysates for use in flavoring foods and beverages.
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Fab fragments are generated by cleavage of IgG with papain instead of pepsin.
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A rapid non-invasive pepsin diagnostic called Peptest is now available which determines the presence of pepsin in saliva samples.
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It works in conjunction with the parietal cell, which releases gastric acid, converting the pepsinogen into pepsin.
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1-bis(diazoacetyl)-2-phenylethane reversibly inactivates pepsin at pH 5, a reaction which is accelerated by the presence of Cu(II).
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Pepsin is expressed as a zymogen called pepsinogen, whose primary structure has an additional 44 amino acids.
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Pepsin's proenzyme, pepsinogen, is released by the chief cells in the stomach wall, and upon mixing with the hydrochloric acid of the gastric juice, pepsinogen activates to become pepsin.
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Pepsins should be stored at very low temperatures (between −80 °C and −20 °C) to prevent autolysis (self-digestion).
Permisi, pak?WikiMatrix WikiMatrix
Therefore, pepsin in solution of up to pH 8.0 can be reactivated upon re-acidification.
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Pepsin is an aspartic protease, using a catalytic aspartate in its active site.
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Pepsin is one of the primary causes of mucosal damage during laryngopharyngeal reflux.
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Pepsin is an endopeptidase that breaks down proteins into smaller peptides (that is, a protease).
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Pepsin in airway specimens is considered to be a sensitive and specific marker for laryngopharyngeal reflux.
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The American microbiologist/vaccinologist Maurice Hilleman at Merck used three treatments (pepsin, urea and formaldehyde) of blood serum together with rigorous filtration to yield a product that could be used as a safe vaccine.
Aturan praktisnya adalah, beratnya minimal lima kali lebih berat dari binatang targetWikiMatrix WikiMatrix
Pepstatin is a low molecular weight compound and potent inhibitor specific for acid proteases with a Ki of about 10−10 M for pepsin.
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The receptor by which pepsin is endocytosed is currently unknown.
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Pepsin is most active in acidic environments between 37 °C and 42 °C. Accordingly, its primary site of synthesis and activity is in the stomach (pH 1.5 to 2).
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45 sinne gevind in 6 ms. Hulle kom uit baie bronne en word nie nagegaan nie.