By Nikki Johnston, Robert J. Toohill
Over the last twenty plus years clinicians have famous major problems of the lung, larynx, pharynx, nostril, sinuses and center ear that take place as a result of duo-denogastric refluxate (DGR) extending to those components. whereas it has lengthy been obtrusive that gastric contents reaches the oesophagus and should reason difficulties within the kind of gastroesophageal reflux disorder (GERD) the problems of extra-oesophageal reflux (EER) are more and more inflicting morbidity to sufferers. lately there were easy and scientific reports indicating that different parts of DGR reason harm to extra-oesophageal buildings. the combo of cutting-edge examine and scientific displays of EER make this ebook very precious to people who examine and deal with sufferers.
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Additional resources for Effects, diagnosis and management of extra-esophageal reflux
However, it is possible that this effect is augmented by pepsin, and that acid alone is not harmful. Twenty-four-hour intraesophageal pH monitoring studies show that the majority of reflux episodes occur between pH 2-4, but this pH range is unable to inflict damage even with >3 hours of exposure to healthy rabbit esophagus (8), which has similar characteristics to human esophagus. 1 for at least 30 min without suffering symptoms of GERD (9). The development of GERD requires that contact between the noxious substances in refluxed gastric juice and the esophageal epithelium be of sufficient duration that esophageal defenses are overwhelmed, or that the potency of the refluxate damages a predisposed or already-damaged epithelium (1).
For the enzyme to be able to operate at low pH the pKa of Asp 32 must be very low to maintain it in the –COO- state. This is achieved by the extensive hydrogen bonding and the nature of the surrounding amino acid R-groups . Figure 1. Diagrammatic representation of pepsin structure. A water molecule is held between the two aspartates, in hydrogen bonding distance of the four oxygen atoms of the carboxyl groups, in the correct position to facilitate nucleophilic attack on the substrate peptide bond .
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