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PubMed2002

Detection of pepsin and glucose in tracheal secretions as indicators of aspiration in mechanically ventilated children.

OBJECTIVES: The detection of glucose in tracheal secretions has been used as an indicator of aspiration in mechanically ventilated, tube-fed children. Pepsin detection may be a more specific indicator. We determined the frequency of pepsin and glucose detection in tracheal secretions of mechanically ventilated children and studied the relationships between tracheal secretion pepsin and glucose and clinical evidence of gastroesophageal reflux. DESIGN: Prospective observational study. SETTING: University teaching hospital. PATIENTS: A convenience sample of mechanically ventilated children. INTERVENTIONS: Tracheal secretions were collected at the time of routine endotracheal tube suctioning. Tracheal aspirate glucose concentrations were assessed by using glucose oxidase reagent strips. Tracheal aspirate pepsin was detected by laboratory immunoassay. MEASUREMENTS AND MAIN RESULTS: One hundred tracheal aspirates were collected from 37 children. Pepsin (>or=1 microg/mL) was detected in nine aspirates, and glucose (>or=20 mg/dL) was detected in 59 aspirates. Overall, five (13.5%) patients had at least one pepsin-positive aspirate, and 33 (89%) had at least one glucose-positive aspirate. Patients with at least one pepsin-positive aspirate were more likely to have clinical evidence of gastroesophageal reflux than patients with pepsin-negative aspirates (5 of 5 vs. 9 of 32, p <.01, Fisher's exact test). Tracheal aspirate glucose positivity was unrelated to the administration of tube feedings and gastroesophageal reflux. No relationship between pepsin and glucose positivity was observed. CONCLUSIONS: Pepsin is detectable in tracheal secretions of mechanically ventilated children at risk for aspiration. Elevated glucose concentrations in tracheal secretions can occur by mechanisms other than aspiration of glucose-rich formula. Pepsin may be a more specific marker for aspiration than glucose.

Journal Article↗

PubMed1995

Cholecystokinin is not a physiological regulator of gastric pepsin secretion in rats.

The physiological relevance of cholecystokinin (CCK) in gastric pepsin secretion is unclear, although CCK has been reported to stimulate pepsin secretion in intact animals and in dispersed chief cell. To clarify the physiological role played by this peptide in pepsin secretion, we determined the effects of intravenous infusions of CCK on gastric pepsin release, and investigated the effect of endogenous CCK released by small amounts of trypsin inhibitor on pepsin secretion in conscious rats. The infusion of CCK-8 at 1 nmol/kg per h resulted in a plasma CCK concentration of 204 pM and a 2.5-fold increase in pepsin secretion compared to the baseline rate. The infusion of CCK-8 at 0.3 nmol/kg per h resulted in a plasma CCK concentration of 41.8 pM and also caused a significant increase in pepsin secretion compared to the baseline rate. However, the infusion of CCK-8 at 0.1 nmol/kg per h (plasma CCK level, 19.9 pM), which is still far beyond the physiological plasma levels of CCK, did not significantly affect pepsin secretion. In addition, the intraduodenal infusion of soybean trypsin inhibitor increased the plasma CCK concentration to 4.4 pM, a value comparable to that observed after feeding (3.3 pM), but again, this had no effect on gastric pepsin secretion. We conclude that CCK is not a physiological regulator of gastric pepsin secretion in rats.

Animals↗

PubMed2004

Gene amplification and cold adaptation of pepsin in Antarctic fish. A possible strategy for food digestion at low temperature.

Cold-adapted organisms have developed a number of adjustments at the molecular level to maintain metabolic functions at low temperatures. Among other features, they can produce enzymes characterized by a high turnover number or a high catalytic efficiency. The present work is aimed at investigating the process of food digestion at low temperature through the study of pepsins in Antarctic notothenioids. For such a purpose, we have cloned and sequenced three forms of pepsin A and a single form of gastricsin from the gastric mucosa of Trematomus bernacchii (rock cod). Phylogenetic analysis has suggested that the three pepsin A isotypes arose from two gene duplication events leading to the most ancestral pepsin A3 and to the most recent forms represented by pepsin A1 and pepsin A2. Molecular modeling has unraveled significant structural differences in these enzymes with respect to their mesophilic counterparts. Hydropathy and flexibility determined on the substrate-binding subsites of Antarctic and mesophilic pepsins have shown for pepsin A2 reduced hydropathy and increased flexibility at the level of the substrate cleft, features typical of cold-adapted enzymes. Northern blot analysis of RNA from rock cod gastric mucosa hybridized with molecular probes designed on specific regions of different pepsin forms has shown that rock cod pepsin genes are expressed at comparable levels. The present results suggest that the Antarctic rock cod adopted two different strategies to accomplish efficient protein digestion at low temperature. One mechanism is the gene duplication that increases enzyme production to compensate for the reduced kinetic efficiency, the other is the expression of a new enzyme provided with features typical of cold-adapted enzymes.

Acclimatization↗

PubMed2004

Effects of pulsed electric fields on the activity and structure of pepsin.

A continuous pulsed electric field (PEF) system integrated with six co-field flow PEF treatment chambers was used to study the inactivation of pepsin. The inactivation of pepsin activity was a function of applied electric field strength, electrical conductivity, and pH. The inactivation of pepsin by PEF followed a first-order model. The first-order inactivation kinetic constant of pepsin was 0.012 (1/mus) in 7.5 mM HCl (pH 2.0) at 34.2 kV/cm. Aggregation of pepsin was observed during PEF treatment; however, the inactivation took place before the formation of aggregates. Circular dichroism analysis showed that inactivation of pepsin by PEF was correlated to the loss of beta-sheet structure in a pepsin molecule. The relative residual activity of PEF-treated pepsin was correlated to the relative molar ellipticity at 215 nm. Both PEF- and heat-induced inactivation of pepsin were correlated with the alteration of the secondary structure (beta-sheet dominant structure) of pepsin.

Circular Dichroism↗

PubMed1970

The pepsins from human gastric mucosal extracts.

1. The pepsins and pepsinogens of the gastric mucosal extracts of two normal subjects, of seven patients with gastric adenocarcinoma and of two patients with duodenal ulcer have been investigated by agar-gel electrophoresis and by ion-exchange chromatography. 2. Of the eight zones of proteolytic activity that have previously been reported in normal human gastric juice, seven can be detected in activated fundic mucosal extracts. Of these seven, four can be attributed to discrete pepsins, numbered 1, 3a, 3 and 5. 3. Zone 7 results from the activity of one or more enzymes that are alkali-stable and are best referred to as gastric proteinases rather than as pepsins. Zone 7 is much more evident in mucosal extracts than in gastric juice. 4. Zones 4 and 6 may result respectively from the activity of a pepsin-inhibitor complex and of an unactivated zymogen. 5. It was not possible, by the chromatographic methods employed, to separate satisfactorily the individual pepsins from activated extracts or their precursors from unactivated extracts, so that the ascribing of a pepsin to a specific zymogen must be considered tentative. Even so, pepsin 3 appears to arise from at least two major precursors, if not from three, whereas pepsins 1 and 5 each arise from a single major precursor. 6. Pyloric mucosal extracts contain principally zone 5 but also zones 6 and 7. These zones in general behave similarly to the corresponding zones of fundic extracts, but pyloric pepsin 5 migrates slightly faster on agar-gel electrophoresis than does fundic pepsin 5 and is a different enzyme. Zones 1 to 4 are absent.

Adenocarcinoma↗

PubMed1978

Ovalbumin digestion by human pepsins 1, 3 and 5.

1. Of the three major human pepsins, pepsin 1 has greater proteolytic activity towards ovalbumin than has pepsin 3. Pepsin 5 has low activity towards this substrate. 2. Proteolytic pH-activity curves show only on pH maximum, about pH 1.4 for pepsin 1, pH 1.4--1.5 for pepsin 3 and pH 1.2--1.4 for pepsin 5. The curve for pepsin 3 has a shoulder between pH 2.4 and 3.4. 3. The rate of digestion of ovalbumin by pepsin 1 is approximately three times slower than are those of bovine haemoglobin or human globin. 4. The results suggest that there may be a physiological advantage in having more than one pepsin.

Electrophoresis, Agar Gel↗

PubMed1976

Pepsinogens and pepsins from gastric mucosa of Japanese Monkey. Purification and characterization.

Five pepsinogens were purified from gastric mucosa of Japanese monkey by DEAE-cellulose column chromatography and Sephadex G-100 gel filtration. Each was shown to be homogeneous by polyacrylamide disc gel electrophoresis. They were designated as pepsinogens I, II, III-1, III-2, and III-3, respectively, based on the elution profile on DEAE-cellulose chromatography. The molecular weights of pepsinogens I and II were 48,000 and 43,000, respectively, and those of the other three were 40,000. Each pepsinogen was converted to pepsin [EC 3.4.23.1] by acidification, and some characteristics, e.g. the pH dependence of activity, sensitivity to various inhibitors, stability to alkali, and hydrolytic activity toward N-acetyl-L-phenylalanyl-3,5-diiodo-L-tyrosine (APDT), were determined. The characteristics of pepsins I and II were the same, and those of pepsins III-1, III-2, and III-3 were similar. Pepsin III-3 showed high stability to alkali (pH 8.0), while the others were less stable. Each pepsin hydrolyzed APDT and was inhibited by acid protease-specific inhibitors, e.g. pepstain, diazoacetyl-DL-norleucine methyl ester (DAN), 1,2-epoxy-3-(p-nitrophenoxy)propane (EPNP), and p-bromophenacyl bromide. The compositions of pepsins I and II were the same, indicating that they are the same protein, and those of pepsins III-1, III-2, and III-3 resembled that of human pepsin. The diversity of pepsinogens and pepsins is discussed in comparison with pepsinogens and pepsins from other animals.

Amino Acids↗

PubMed2004

Pepsin and carbonic anhydrase isoenzyme III as diagnostic markers for laryngopharyngeal reflux disease.

OBJECTIVES/HYPOTHESIS: The objective was to investigate the potential use of pepsin and carbonic anhydrase isoenzyme III (CA-III) as diagnostic markers for laryngopharyngeal reflux disease. STUDY DESIGN: Prospective cell biological investigation was conducted of laryngeal biopsy specimens taken from 9 patients with laryngopharyngeal reflux disease and 12 normal control subjects using antibodies specific for human pepsin (produced in the authors' laboratory within the Department of Otolaryngology at Wake Forest University Health Sciences, Winston-Salem, NC) and CA-III. METHODS: Laryngeal biopsy specimens were frozen in liquid nitrogen for Western blot analysis and fixed in formalin for pepsin immunohistochemical study. Specimens between two groups (patients with laryngopharyngeal reflux disease and control subjects) were compared for the presence of pepsin. Further analyses investigated the correlation between pepsin, CA-III depletion, and pH testing data. RESULTS: Analysis revealed that the level of pepsin was significantly different between the two groups (P < .001). Secondary analyses demonstrated that presence of pepsin correlated with CA-III depletion in the laryngeal vocal fold and ventricle (P < .001) and with pH testing data in individuals with laryngopharyngeal reflux disease. CONCLUSION: Pepsin was detected in 8 of 9 patients with laryngopharyngeal reflux disease, but not in normal control subjects (0 of 12). The presence of pepsin was associated with CA-III depletion in the laryngeal vocal fold and ventricle. Given the correlation between laryngopharyngeal reflux disease and CA-III depletion, it is highly plausible that CA-III depletion, as a result of pepsin exposure during laryngopharyngeal reflux, predisposes laryngeal mucosa to reflux-related inflammatory damage.

Biomarkers↗

PubMed2005

Sensitive pepsin immunoassay for detection of laryngopharyngeal reflux.

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 period for pepsin measurement using enzyme-linked immunoadsorbent assay. RESULTS: Pepsin assay results from 63 throat sputum samples obtained from 23 study subjects were compared with their pH monitoring data. Twenty-two percent (14/63) of the sputum samples correlated the presence of pepsin with LPR (pH < or = 4 at the pharyngeal probe), of which the median concentration of pepsin was 0.18 microg/mL (range 0.003-22 microg/mL). Seventy-eight percent (49/63) of the samples unassociated with (pharyngeal) reflux contained no detectible pepsin. Mean pH values for pepsin-positive samples were significantly lower than negative samples at both esophageal probe (pH 2.2 vs. pH 5.0) (P < .01) and the pharyngeal probe (pH 4.4 vs. pH 5.8) (P < .01). When the pepsin assay results were compared with the pharyngeal pH data for detecting reflux (events pH < or = 4), the pepsin immunoassay was 100% sensitive and 89% specific for LPR. CONCLUSIONS: Detection of pepsin in throat sputum by immunoassay appears to provide a sensitive, noninvasive method to detect LPR.

Acid-Base Equilibrium↗

PubMed2006

Pepsin, a reliable marker of gastric aspiration, is frequently detected in tracheal aspirates from premature ventilated neonates: relationship with feeding and methylxanthine therapy.

OBJECTIVES: To determine the frequency of pepsin detection in tracheal aspirate (TA) samples of mechanically ventilated premature neonates and its association with feedings and methylxanthine therapy. PATIENTS AND METHODS: Serial TA samples (days 1, 3, 5, 7, 14, 21, 28 and >28 days) were collected from premature neonates receiving ventilatory support. An enzymatic assay with a fluorescent substrate was used to detect pepsin. Pepsin was also measured in 10 serum samples collected in conjunction with the TA samples from 8 neonates. RESULTS: A total of 239 TA samples was collected from 45 premature neonates (mean birth weight, 762 +/- 166 g; mean gestational age, 25.5 +/- 1.5 wk). Pepsin was detectable in 222 of 239 TA samples (92.8%) and in none of the serum samples. Pepsin was significantly lower on day 1 (mean, 170 +/- 216 ng/mL) when compared with all other time points (P < 0.05). Mean concentration of pepsin was significantly lower when infants were unfed (265 +/- 209 ng/mL) compared with levels during feeding (390 +/- 260 ng/mL, P = 0.02). The mean level of pepsin was significantly higher in infants during xanthine therapy (419 +/- 370 ng/mL) compared with no xanthine therapy (295 +/- 231 ng/mL, P = 0.037). CONCLUSION: Pepsin, a marker of gastric contents, was detected in more than 92% of TA samples from premature infants on mechanical ventilation. The level of pepsin was higher in fed infants when compared with unfed infants. Xanthine therapy was also associated with increased pepsin in TA samples. Chronic aspiration of gastric contents may worsen lung disease in premature infants.

Aging↗

PubMed2005

IgE binding to pepsin-digested food extracts.

BACKGROUND: Pepsin resistance of allergens like lipid transfer protein and 2S albumin has been suggested as explanation for the severity of symptoms often induced by these allergens. Component-resolved diagnosis with purified labile and stable allergens has therefore been proposed to better characterize the risk involved in a positive in vitro IgE test. However, for many foods, purified allergens are not (yet) available. OBJECTIVE: It was the aim of this study to evaluate the potential of pepsin-digested whole-food extracts to distinguish between IgE responses to stable (potentially severe) and labile (mild) allergens. METHODS: Sera (n = 143) from Italian, Spanish and Dutch patients with hazelnut and/or apple ingestion-related symptoms were analyzed for residual IgE binding to pepsin-resistant hazelnut and/or apple allergens. Control and pepsin-digested hazelnut and apple extracts were used for radioallergosorbent test analysis and immunoblot analysis. RESULTS: Pepsin digestion of food extracts, like from hazelnut and apple used for in vitro diagnostic tests, provides a way to distinguish sensitization to pepsin-resistant allergens from that to pepsin-susceptible allergens. In this selected group of patients, IgE reactivity to pepsin-digested extracts correlated with sensitization to the stable allergen lipid transfer protein. The analysis further revealed that the use of soluble pepsin can result in false-positive in vitro tests (2/143). CONCLUSION: Pepsin-digested food extracts are a convenient tool to identify patients with IgE antibodies against potentially dangerous stable allergens, in particular for those foods where the relevant stable allergens have not yet been identified. This can increase the clinical prognostic value of food allergy serology.

Allergens↗

PubMed1985

Serum pepsin activity as a parameter of gastric acid secretion.

Serum pepsin activity was measured in 359 patients with various gastric diseases, the serum protein themselves serving as substrate. In 332 out of 359 patients, BAO and PAO, and in 173 of these patients, pepsin activity, were determined in gastric juices. In 102 patients, serum pepsin activity was measured before, and 45 and 90 minutes after, pentagastrin stimulation. In 71 out of these 102 patients, pepsinogen I was measured simultaneously by RIA. There was good correlation between stimulated serum pepsin activity and maximal pepsin output (r = 0.63), as well as BAO (r = 0.67) and PAO (r = 0.77). The higher the PAO, the greater the increase in pepsin activity in the sera after pentagastrin stimulation. The increase in pepsinogen I under stimulation was smaller in the sera than pepsin activity. There was a slightly better correlation of PAO with stimulated serum pepsin activity than with pepsinogen I (r = 0.76 versus 0.62). The measurement of pentagastrin-stimulated pepsin activity in sera, as a very simple and inexpensive method, permits the screening, with an overall accuracy of more than 75%, of achlorhydrics (stimulated pepsin activity less than 30 micrograms thyrosine/24 hours/ml serum), acid secretors (greater than 80 micrograms thyrosine/24 hours/ml serum) and hypersecretors (PAO greater than 35 mmol HCl/hours, greater than 120 micrograms thyrosine/24 hours/ml serum).

Achlorhydria↗

PubMedDate not supplied

[Intramolecular mobility of pepsin].

By modifying four tyrosine residues in pepsin a derivative (aminopepsin) is obtained which is capable to conjugate with a fluorescent label DNS-Cl without loss of the catalytic activity. Rotational relaxation times of native pepsin and dansylated aminopepsin (DAP) are measured by a fluoresence polarization method. The values obtained are shown to be lower than those calculated for arigid pepsin globule. Possible sources of the obtained difference are discussed. A reversible or covalent blocking of pepsin or DAP active centres by specific inhibitors leads to an increase in rotational relaxation time values for these proteins reaching the magnitude which is very close to that calculated for a model of rigid pepsin. Brownian relaxation of pepsin and DAP reduced by beta-mercaptoethanol and of pepsinogen and some fragments of pepsine macromolecule in aqueous solutions is invigated as well. The results are intepreted as representing an intramolecular mobility or segmental flexibility of pepsin and DAP. With the use of the obtained and X-ray data a segmental model of dynamic pepsin structure is suggested. On the basis of this model some conclusions are drawn concerning a localization of a polypeptide which is split off from the N-terminus of pepsinogen during its activation. A possible role of segmental flexibility in the catalytic action of pepsin is considered.

Animals↗

PubMed1980

Exogenous and endogenous acid and pepsins in the pathogenesis of duodenal ulcers in the rat.

A continuous subcutaneous infusion for 24 hr of the gastric secretagogues, pentagastrin (4 micrograms/kg/min) together with carbachol (0.8 micrograms/kg/min) produced a 100% incidence of duodenal ulcers (DU) in male albino Wistar rats. The mean acid output producing these duodenal ulcers was 2.3 mmol/24 hr, with a gastric secretory volume of 25 (+/- 1) ml/24 hr at an acid concentration of 91 (+/- 2) mmol/liter. The pepsin activity in the gastric juice was 185 micrograms/ml. To simulate this acid-pepsin hypersecretion, acid and/or pepsin was infused intragastrically for 24 hr. The intragastric infusion of hydrochloric acid (0.1 M, 0.2 M, 0.5 M) alone and hog purified pepsin (2.5, 5, 10 mg/24 hr) at a constant rate of 1 ml/hr for 24 hr failed to produce duodenal ulcers in rats although gastric lesions in the body of the stomach were produced. The infusion of 0.2 M HCl with 5 mg pepsin over 24 hr produced DU in two of 10 rats. However, pooled secretagogue-stimulated gastric juice, infused intragastrically, produced DUs in 11 of 12 rats. Acid alone does not produce DU experimentally in rats at the rate of infusion used in these experiments. Acid and exogenous procine pepsin (similar to human pepsin 3 on agar gel electrophoresis) rarely produced duodenal ulcers. However, acid and endogenous rat pepsin are needed together for the duodenal ulcerogenesis. This pepsin may be an obligatory ulcerogenic factor in the rat.

Animals↗

PubMed1980

Purificaton and characterization of a pepsinogen and its pepsin from proventriculus of the Japanese quail.

A crude extract of the proventriculus of the Japanese quail gave at least five bands of peptic activity at pH 2.2 on polyacrylamide gel electrophoresis. The main component, constituting about 40% of the total acid protease activity, was purified to homogeneity by hydroxyapatite and DEAE-Sepharose column chromatographies. At below pH 4.0, the pepsinogen was converted to a pepsin, which had the same electrophoretic mobility as one of the five bands of peptic activity present in the crude extract. The molecular weights of the pepsinogen and the pepsin were 40 000 and 36 000, respectively. Quail pepsin was stable in alkali up to pH 8.5. The optimal pH of the pepsin on hemoglobin was pH 3.0. The pepsin had about half the milk-clotting activity of purified porcine pepsin, but the pepsinogen itself had no activity. The hydrolytic activity of quail pepsin on N-acetyl-L-phenylalanyl-3,5-diiodo-L-tyrosine was about 1% of that of porcine pepsin. Among the various protease inhibitors tested, only pepstatin inhibited the proteolytic activity of the pepsin. The amino acid composition of quail pepsinogen was found to be rather similar to that of chick pepsinogen C, and these two pepsinogens possessed common antigenicity.

Animals↗

PubMed1990

Molecular characteristics of pepsinogen and pepsin from duck glandular stomach.

1. Two procedures were developed for the preparation of duck pepsinogen, an enzyme from the family of aspartic proteases (EC 3.4.23.1) and its zymogen. 2. The amino acid composition, sugar content and the partial N- and C-terminal sequences of both the enzyme and the zymogen were determined. These sequences are highly homologous with the terminal sequences of chicken pepsin(ogen). 3. Duck pepsinogen and pepsin are unlike other pepsin(ogen)s in being relatively stable in alkaline media: pepsinogen is inactivated at pH 12.1, pepsin at pH 9.6. 4. Duck pepsin is inhibited by diazoacetyl-D,L-norleucine methyl ester (DAN), 1,2-epoxy-3(p-nitrophe-noxy)propane (EPNP), pepstatin and a synthetic pepsin inhibitor Val-D-Leu-Pro-Phe-Phe-Val-D- Leu. The pH-optimum of duck pepsin determined in the presence of synthetic substrate is pH 4. 5. Duck pepsin has a marked milk-clotting activity whereas its proteolytic activity is lower than that of chicken pepsin. 6. The activation of duck pepsinogen is paralleled by two conformational changes. The activation half-life determined in the presence of a synthetic substrate at pH 2 and 14 degrees C is 20 sec.

Amino Acid Sequence↗

PubMed2005

Use of enhanced green fluorescent protein to determine pepsin at high sensitivity.

A fluorometric assay for pepsin and pepsinogen was developed using enhanced green fluorescent protein (EGFP) as a substrate. Acid denaturation of EGFP resulted in a complete loss of fluorescence that was completely reversible on neutralization. In the proteolytic assay procedure, acid-denatured EGFP was digested by pepsin or activated pepsinogen. After neutralization, the remaining amount of undigested EGFP refolded and was determined by fluorescence. Under standard digestion conditions, 4.8-24.0 ng pepsin or pepsinogen was used. Using porcine pepsin as a standard, 38+/-6.7 ng EGFP was digested per min-1 ng pepsin-1. Activated porcine pepsinogen revealed a similar digestion rate (37.2+/-5.2 ng EGFP min-1 ng activated pepsinogen-1). The sensitivity of the proteolysis assay depended on the time of digestion and the temperature. Increasing temperature and incubation time allowed quantification of pepsin or pepsinogen in a sample even in the picogram range. The pepsin-catalyzed EGFP digestion showed typical Michaelis-Menten kinetics. Km and Vmax values were determined for the pepsin and activated pepsinogen. Digestion of EGFP by pepsin revealed distinct cleavage sites, as analyzed by SDS-PAGE.

Animals↗

PubMed2004

A new pepsin assay to detect pulmonary aspiration of gastric contents among newly intubated patients.

Aspiration of gastric contents by endotracheally intubated patients is associated with significant morbidity and mortality. Previous studies suggest that pepsin in tracheal aspirates may be a valuable marker of occult aspiration. We sought to show the sensitivity and specificity of a new, pepsin-specific assay in humans. A prospective, case-controlled study was conducted with subjects serving as their own controls. After planned endotracheal and nasogastric intubation for elective surgery, 20 participants had tracheal and gastric aspirates withdrawn. A blinded investigator tested samples for the presence of pepsin using the assay. Positive samples were then tested with pepstatin, a specific pepsin inhibitor, to ensure that positive results were due to pepsin. All tracheal aspirates tested negative and all gastric aspirates tested positive for pepsin. Pepstatin halted pepsin activity in all positive samples, ensuring that positive results were due to pepsin. A pepsin-specific assay is extremely reliable for detecting gastric contents in humans.

Adult↗