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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Evaluation of the binding affinity and antioxidant activity of phlorizin to pepsin and trypsin [PDF]
Food Science and Human Wellness, 2023 Phlorizin (PHL) is a natural compound with strong antioxidant properties mainly found in apples. In this paper, the interaction mechanism of PHL with pepsin and trypsin was comparatively evaluated by computer simulation, fluorescence spectra, circular ...
Jing Zhang +7 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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Antibacterial activity of a pepsin‐derived bovine hemoglobin fragment [PDF]
FEBS Letters, 2001 Peptic digestion of bovine hemoglobin yields a fragment with antibacterial activity. This peptide was purified to homogeneity by a two‐step procedure including anion exchange chromatography and preparative reversed‐phase HPLC. Mass determination and fragmentation indicated that this peptide corresponded to the 1–23 fragment of the α chain of hemoglobin.
Rénato Froidevaux +7 more
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Pepsin Digestion for Proteomic Studies of the Human Hair Shaft. [PDF]
Rapid Commun Mass SpectromYee DH +4 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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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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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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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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