Gastric acid secretion, pepsin secretion, and fasting serum gastrin levels were measured in 23 patients with duodenal ulcer disease, divided into three groups which received either cimetidine 800 mg daily, cimetidine 1600 mg daily, or ranitidine hydrochloride 300 mg daily for eight weeks. Pentagastrin tests were carried out at intervals both before and after treatment. Each dose of cimetidine r...

IN a recent series of publications Northrop [1930, 1, 2; 1931] has advanced very strong evidence that pepsin is a protein. Starting from commercial pepsin, by suitably regulating the pH and precipitating with the aid of magnesium or ammonium sulphate a crystalline product was obtained which had the general properties of a protein. In particular, solutions of this crystalline pepsin were coagula...

The utilization of industrial sunflower meal to produce protein-rich products for the food industry is an alternative approach for better and more efficient use of this agricultural by-product. Sunflower meal proteins possess specific functional properties, which however need improvement to broaden their potential as supplements for delivering high--quality products for human nutrition. The aim...

We have studied the effect of a prostaglandin E2 analogue (enprostil), on intragastric acidity, gastric acid and pepsin outputs during a 24 hour period in nine patients with duodenal ulcer in remission. Enprostil 35 micrograms bd dose inhibited 24 hour intragastric acidity by 38% and a 70 micrograms nocturnal dose by 33%. Decrease in nocturnal pepsin secretion was both volume and concentration ...

A previous paper (2) described the isolation and crystallization of gastricsin from human gastric juice and the physical, chemical, and enzymatic properties of gastricsin as compared to human pepsin. It is the purpose of the present report to describe the purification and properties of a zymogen from human gastric mucosa. The activation of this zymogen produces both gastricsin and human pepsin.

Butane-2,3-dione inactivates the aspartyl proteinases from Penicillium roqueforti and Penicillium caseicolum, as well as pig pepsin, penicillopepsin and Rhizopus pepsin, at pH 6.0 in the presence of light but not in the dark. The inactivation is due to a photosensitized modification of tryptophan and tyrosine residues. In the dark none of the amino acid residues, not even arginine residues, is ...

Peptide mapping of antibodies is an essential method to monitor peptide modifications in antibody lots that could affect the safety and efficacy product. Conventional protocols rely on protein digestion using proteases, such as trypsin, before with mass spectrometry (MS). However, trypsin may cause incomplete peptides, especially those include highly hydrophobic peptides. Here, we show how peps...

Evidence relating to the structure and properties of swine pepsinogen and pepsin has been reviewed and used to suggest a tentative two dimensional picture of the skeleton of these two proteins. When pepsinogen, a folded single peptide chain, is converted to pepsin, there is a profound change in the physical and chemical properties of the protein. In an as yet unknown manner, except that it is i...