Effect of proteolytic enzymes and polypeptides on the antacid activity of almagate and other antacids.
The acid neutralizing capacity of almagate (hydrated aluminium-magnesium hydroxycarbonate, Al2Mg6(OH)14(CO3)2 X 4H2O, Almax), magaldrate and an aluminium-magnesium hydroxide cogel was measured in the presence of different concentrations of pepsin or peptone. The crystalline antacids, almagate and magaldrate, when tested in the absence of polypeptides were less active acid neutralizing agents than the aluminium-magnesium hydroxide cogel but in the presence of the polypeptides they were considerably more active, especially in respect of time of neutralization. In the presence of pepsin, almagate was considerably more active than in the absence of this enzyme, whereas magaldrate suffered little change in activity and the dried aluminium-magnesium cogel was less active. The results demonstrate the importance of measuring acid neutralizing capacity in presence of naturally occurring polypeptides.
D000536:Aluminum Hydroxide / Q000494:pharmacology*; D000863:Antacids / Q000494:pharmacology*; D002254:Carbonates / Q000494:pharmacology*; D004347:Drug Interactions; D005744:Gastric Acid / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D008274:Magnesium / Q000494:pharmacology*; D008276:Magnesium Hydroxide / Q000494:pharmacology*; D010447:Peptide Hydrolases / Q000494:pharmacology*; D010455:Peptides / Q000494:pharmacology*; D013997:Time Factors
D000863:Antacids; D002254:Carbonates; D010455:Peptides; C043698:almagate; D000536:Aluminum Hydroxide; D010447:Peptide Hydrolases; D008274:Magnesium; D008276:Magnesium Hydroxide