Pepsin properties, structure, and its accurate measurement: a narrative review
نویسندگان
چکیده
: Pepsin is an aspartate protease that generated from its proenzyme, pepsinogen by autocatalysis initiated a fall in pH below 5. Human gastric juice contains eight isoenzymes of pepsin. The peptides released on conversion to pepsin which there are potentially five, have been shown antimicrobial activity against wide range bacteria including Escherichia coli, Pseudomonas and Staphylococcus also biofilm formation inhibiting properties. stability response changes varies between pepsinogen. Pepsinogen stable up 10, only just above 7.0 completely denatured at 8.0. Many diseases the aerodigestive tract linked reflux presence Therefore, measurement tissue lavages or saliva sputum, could be good screening tool for diagnosis related disease. However, no current consensus as best methods measure it time sample it. For effective enzyme-linked immunosorbent assay (ELISA), following required; monoclonal/monospecific polyclonal antibody with lowest level detection (LLOD) sensitivity 1–25 ng/mL (depending dilution) adequate supply purified human standard antibody-based assays. If possible, should used protein does not indicate capable damaging activity. Finally, if associated disease large studies required confirm multiple samples. This review deals several where quantitation attempted, their techniques assessed.
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ژورنال
عنوان ژورنال: Annals of esophagus
سال: 2022
ISSN: ['2616-2784']
DOI: https://doi.org/10.21037/aoe-20-95