نتایج جستجو برای: gastri pepsin

تعداد نتایج: 3046  

Journal: :The Laryngoscope 2007
Nikki Johnston Peter W Dettmar Bimjhana Bishwokarma Mark O Lively Jamie A Koufman

OBJECTIVES/HYPOTHESIS Exposure of laryngeal epithelia to pepsin during extra-esophageal reflux causes depletion of laryngeal protective proteins, carbonic anhydrase isoenzyme III (CAIII), and squamous epithelial stress protein Sep70. The first objective of this study was to determine whether pepsin has to be enzymatically active to deplete these proteins. The second objective was to investigate...

Journal: :Poultry science 2015
T M Davis C M Parsons P L Utterback D Kirstein

Sixteen meat and bone meal (MBM) samples were obtained and selected from various company plants to provide a wide range in pepsin nitrogen digestibility values. Pepsin digestibility was determined using either 0.02 or 0.002% pepsin. Amino acid (AA) digestibility of the 16 MBM samples was then determined using a precision-fed cecectomized rooster assay. The 0.02% pepsin digestibility values were...

Journal: :The Yale Journal of Biology and Medicine 1999
B. I. Hirschowitz

Esophagitis results from excessive exposure of the esophagus to gastric juice through an ineffective or dysfunctional lower esophageal sphincter mechanism. A possible role of pepsin in damaging the esophageal mucosa with consequent esophagitis may be examined directly by testing pepsin under various conditions in experimental models of esophagitis. Since gastric juice contains both acid and pep...

Journal: :The Journal of General Physiology 1963
Helen Van Vunakis Harris I. Lehrer William S. Allison Lawrence Levine

Rabbit antisera to pepsin and pepsinogen were characterized by several immunological criteria. Both antisera inhibited the rennet activity of pepsin. Antipepsinogen protected pepsin from alkaline denaturation. Using antipepsinogen, precipitin analysis at pH 5.5 indicated that the native enzyme resembles the precursor more closely than did the denatured enzyme. However, all three proteins have s...

Journal: :Gut 1979
V Walker W H Taylor

Pure human pepsins 1 and 3 are inactivated by incubation at pH 7.1-7.3 for 30 minutes, losing 90% or more of activity. Pepsin 5 is alkali-stable, retaining 100% of activity. Mixtures of pure pepsins 1 and/or 3 with pepsin 5 were found to have greater alkali-stable activity than predicted. Two published methods for determining the alkali-stable fraction of the peptic activity of gastric juice ga...

2015
Usha Krishnan Shaun Rama Isabella Messina Emily Horsley

Research Motivation: Gastroesophageal reflux disease (GERD) is a well-recognised cause of respiratory symptoms in children. Confirming a diagnosis of reflux aspiration remains difficult, due to limitations in currently available investigations. The presence of pepsin in respiratory secretions has been documented in literature as a marker of reflux aspiration; however the correlation of pepsin a...

Journal: :The Laryngoscope 2005
John Knight Mark O Lively Nikki Johnston Peter W Dettmar Jamie A Koufman

OBJECTIVES/HYPOTHESIS To determine whether measurement of pepsin in throat sputum by immunoassay could be used as a sensitive and reliable method for detecting laryngopharyngeal reflux (LPR) compared with 24-hour double-probe (esophageal and pharyngeal) pH monitoring. STUDY DESIGN Patients with clinical LPR undergoing pH monitoring provided throat sputum samples during the reflux-testing peri...

Journal: :The Journal of General Physiology 1938
Roger M. Herriott Quentin R. Bartz John H. Northrop

Activation of swine pepsinogen with chicken pepsin results in the formation of swine pepsin. Activation of chicken pepsinogen with swine pepsin results in the formation of chicken pepsin. The structure responsible for the species specificity of the enzyme is therefore present in the inactive precursor.

Journal: :The Journal of General Physiology 2003
John H. Northrop

A protein fraction has been isolated from crude pepsin preparations which is about 400 times as active as crystalline pepsin in the lique-faction of gelatin. The activity as measured by the digestion of casein, edestin or egg albumin is less than that of crystalline pepsin. It is more resistant to alkali than the crystalline pepsin.

Journal: :Gut 1990
H P Tay R C Chaparala J W Harmon J Huesken N Saini F Z Hakki E J Schweitzer

Bismuth subsalicylate was tested in an in vivo perfused rabbit model of oesophagitis for its ability to prevent the mucosal injury caused by pepsin. Treatment efficacy was assessed under both a treatment-before-injury protocol and a treatment-after-injury protocol. Oesophageal mucosal barrier function was evaluated by measuring flux rates of H+, K+, and glucose. The degree of oesophagitis was d...

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