pepsin


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pep·sin

also pep·sine  (pĕp′sĭn)
n.
1. A digestive enzyme found in gastric juice that catalyzes the breakdown of protein to peptides.
2. A substance containing pepsin, obtained from the stomachs of hogs and calves and used as a digestive aid.

[Greek pepsis, digestion (from peptein, to digest; see pekw- in Indo-European roots) + -in.]

pepsin

(ˈpɛpsɪn) or

pepsine

n
(Biochemistry) a proteolytic enzyme produced in the stomach in the inactive form pepsinogen, which, when activated by acid, splits proteins into peptones
[C19: via German from Greek pepsis, from peptein to digest]

pep•sin

(ˈpɛp sɪn)

n.
1. an enzyme, produced in the stomach, that in the presence of hydrochloric acid splits proteins into proteoses and peptones.
2. a commercial preparation containing pepsin, obtained from hog stomachs, used chiefly as a digestive and as a ferment in making cheese.
[1835–45; < Greek péps(is) digestion (pep-, base of péptein to digest + -sis -sis) + -in1]

pep·sin

(pĕp′sĭn)
A powerful enzyme that breaks down proteins in the stomach of vertebrate animals.

pepsin

A protein-digesting enzyme in the stomach.
ThesaurusAntonymsRelated WordsSynonymsLegend:
Noun1.pepsin - an enzyme produced in the stomach that splits proteins into peptones
gastric acid, gastric juice - digestive secretions of the stomach glands consisting chiefly of hydrochloric acid and mucin and the enzymes pepsin and rennin and lipase
enzyme - any of several complex proteins that are produced by cells and act as catalysts in specific biochemical reactions
Translations

pepsin

[ˈpepsɪn] Npepsina f

pepsin

nPepsin nt

pepsin

[ˈpɛpsɪn] npepsina

pep·sin

n. pepsina, enzima principal del jugo gástrico.

pepsin

n pepsina
References in classic literature ?
Between blasts she resorted to Epictetian philosophy in the form of pepsin chewing gum.
They had curled-hair works for the cattle tails, and a "wool pullery" for the sheepskins; they made pepsin from the stomachs of the pigs, and albumen from the blood, and violin strings from the ill-smelling entrails.
He suffered from dyspepsia, and he might often be seen sucking a tablet of pepsin; in the morning his appetite was poor; but this affliction alone would hardly have impaired his spirits.
In 91% (out of 65) samples from children undergoing myringotomy for OME, pepsin/pepsinogen levels in the middle ear effusion samples were up to 1000 times higher than serum levels, indicating that pepsin in the middle ear was almost certainly due to reflux of gastric contents.
Throughout the culture, larvae samples were homogenized in 200 mg [mL.sup.-1] of the mix of 100 mmol [L.sup.-1] of glycine-HCl buffer pH 2 for acid activity (pepsin) and with Tris-HCl 30 mmol [L.sup.-1] buffer + CaCh 12.5 mM pH 7.5 for alkaline enzyme activity.
Pepsin hydrolysis: Casein ([alpha]-S1) (10 mg) was solubilized in 1mL 0.1M HCl.
In 2012, a study by Koufman and Johnston found that the addition of alkaline drinking water (pH 8.8) instantly denatured pepsin, in addition to acting as an acid buffer.
The pathophysiology of LPR differs somewhat from that of GERD, in that injury to laryngeal tissue appears to be due primarily to pepsin, rather than to acid.
Pepsin was noted to be active in 14.4% of 152 subjects who underwent tympanostomy tube placement [6].
Proteins in cheese are thought to be easily hydrolyzed in a gastric environment because of the presence of hydrochloric acid and pepsin. However, recent findings have shown that this environment may impede the digestion of cheese.
PH, temperature stability, substrate specificity, the substrate of protection, the effect of metal ions, pepsin and trypsin on endo-[beta]-1,4-glucanase activity, were determined as described previously (19), with minor modifications.