Anti-pepsin activity of silicon dioxide nanoparticles [PDF]
Revista Colombiana de Química, 2016 SiO2NPs as an inhibitor of pepsin enzyme for treatment of gastro-esophageal reflux disease (GERD) was used. Silicon dioxide nanoparticles (pepsin coated SiO2NPs) are among the safest nanoparticles that can be used inside the human body.
Hussein Kadhem Al-Hakeim +2 more
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Research note: Extraction, purification, physicochemical, and biochemical properties of pepsin isolated from geese forestomachs fed under intensive and extensive conditions [PDF]
Poultry ScienceThis Research Note reports the isolation and basic characterization of pepsin obtained from the forestomach of geese raised under intensive and extensive rearing systems.
Pelin Beyazgul +7 more
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Combined laryngopharyngeal reflux and obstructive sleep apnea (CLOSA) – Salivary pepsin test for laryngopharyngeal reflux in obstructive sleep apnea patients [PDF]
Tzu Chi Medical JournalObjectives: Reflux disease including gastroesophageal reflux and laryngopharyngeal reflux (LPR) is often found in obstructive sleep apnea (OSA) patients. Endoscopic examination is a gold standard diagnosis for reflux disease.
Shih-Chieh Shen +8 more
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ChemosensorsIn this study, we introduce a novel cleavage reaction lateral flow assay (LFA) based on pepsin activity against a pepsin-susceptible peptide (PSP) substrate to detect salivary pepsin.
Sung-Woong Kang +4 more
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Analyzing pepsin degradation assay conditions used for allergenicity assessments to ensure that pepsin susceptible and pepsin resistant dietary proteins are distinguishable. [PDF]
PLoS ONE, 2017 The susceptibility of a dietary protein to proteolytic degradation by digestive enzymes, such as gastric pepsin, provides information on the likelihood of systemic exposure to a structurally intact and biologically active macromolecule, thus informing on
Rong Wang +8 more
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Separation of pepsin I, pepsin II A, pepsin II B, and pepsin III from human gastric mucosa [PDF]
American Journal of Physiology-Legacy Content, 1963 Extracts of human gastric mucosa have been fractionated on diethylaminoethyl cellulose to yield three precursors of proteolytic enzymes active at low pH which have been called pepsinogen I, pepsinogen II, and pepsinogen III. Pepsinogen I has been found in the mucosa from all parts of the stomach examined as well as in the proximal duodenum. Pepsinogen
M J, SEIJFFERS, H L, SEGAL, L L, MILLER
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Pepsin D. A minor component of commercial pepsin preparations [PDF]
Biochemical Journal, 1967 Methods are described for the isolation and purification of pepsin D, an enzyme which accounts for about 10% of the enzymic activity in commercial preparations of pepsin. Pepsin D is similar to pepsin in having a molecular weight of about 35000, the same C-terminal amino acid sequence, and an N-terminal isoleucine residue.
D, Lee, A P, Ryle
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Effects of pepsin and pepstatin on reflux tonsil hypertrophy in vitro. [PDF]
PLoS ONE, 2018 There is evidence that pepsin can aggravate tonsil hypertrophy. Pepstatin is a potent inhibitor of pepsin activity and could protect patients against reflux tonsil hypertrophy by inhibiting pepsin.
Jin Hyun Kim +4 more
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PLoS ONE, 2020 Pepsin plays an important role in laryngopharyngeal reflux (LPR), a risk factor for the development of hypopharyngeal squamous cell carcinomas (HPSCC). However, the role of pepsin in HPSCC is not clear.
Kai Niu +8 more
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The In Vitro Effect of Acidic-Pepsin on Nuclear Factor KappaB Activation and Its Related Oncogenic Effect on Normal Human Hypopharyngeal Cells. [PDF]
PLoS ONE, 2016 Extra-esophageal carcinogenesis has been widely discussed in relation to the chronic effects of laryngopharyngeal reflux and most prominently with pepsin historically central to this discussion.
Clarence T Sasaki +2 more
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