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Biomedical subjects

Z Szafran

Publications and source records attributed to Z Szafran.

At least 37 records · Page 2Linked to original sources

Blood serum immunoreactive gastrin level in infants with hypertrophic pyloric stenosis.

Blood serum immunoreactive gastrin level (IRG) was measured in infants with hypertrophic pyloric stenosis before and after corrective surgery and in a control group children of corresponding age. No significant difference in IRG level was found between the stenotic infants and the control group. In the stenotic infants IRG values were higher at the seventh day after than before the operation and significantly higher in those infants in whom gain of body weight was noted during that time as compared with the infants without gain of weight. These observations remain in agreement with the view that the main role of gastrin in infants is trophic action on the mucosa of the upper gastrointestinal tract.

Body Weight↗

Esterolytic activity of blood serum in infants with hypertrophic pyloric stenosis.

Esterolytic activity of blood serum was determined in infants with hypertrophic pyloric stenosis and in healthy control children. The substrates hydrolyzed mainly by arylesterase (EC. 3.1.1.2), i.e. p-nitrophenyl esters of acetic, propionic and butyric acid were used. It was found that in infants with hypertrophic pyloric stenosis the rate of p-nitrophenyl propionate hydrolysis was significantly higher than that of the acetate or butyrate. In control group children all three substrates were hydrolysed at similar rates, and these were significantly lower than in infants with hypertrophic pyloric stenosis.

Carboxylic Ester Hydrolases↗

Coupled secretion of gastric lipase and pepsin in man following pentagastrin stimulation.

Secretion patterns of gastric lipase and pepsin were studied in duodenal ulcer patients before and after vagotomy and in healthy subjects following continuous administration of pentagastrin in graded doses. The lipase output increased in response to pentagastrin stimulation in similar fashion as that of pepsin. The output of the two enzymes were correlated with each other and with hydrogen ion output. Evaluation of dose-response relationships showed that in duodenal ulcer patients the secretion of gastric lipase and pepsin is more sensitive to pentagastrin stimulation than that of hydrogen ions.

Adult↗

Electrophoretic properties and specificity of human gastric lipase.

Electrophoretic separation of gastric juice and the homogenate of stomach body mucosa on polyacrylamide gel followed by staining for esterolytic activity resulted in a characteristic zymogram composed of five activity bands located in the cathodal part of the electropherogram. This pattern was lacking in zymograms obtained for the homogenates of antral and duodenal mucosa. Lipolytic activity was confined to the same area of the gel where the five band pattern of esterolytic activity was localized. It was concluded that gastric juice and homogenate of stomach body mucosa contain one esterolytic enzyme of wide specificity, known as gastric lipase.

Duodenum↗

Relationship between undissociated acidity of gastric juice and gastric protein secreted in response to graded doses of pentagastrin in duodenal ulcer patients.

Concentrations of free and total hydrogen ions, total protein and pepsin were measured in gastric juice fractions collected during basal secretion and upon stimulation by graded doses of pentagastrin administered intravenously. Undissociated hydrogen ion and non-pepsin protein concentrations were calculated as derived quantities. The studies were carried out in nine patients with duodenal ulcer both before and after truncal vagotomy. It was found that after vagotomy the undissociated hydrogen ion concentration was significantly lower and non-pepsin protein higher than before the operation. No correlation was found between the two quantities both before and after vagotomy. It was concluded that in duodenal ulcer patients either not all non-pepsin protein takes part in buffering of hydrogen ions secreted by parietal cells, or that non-protein buffers play a more important role.

Adult↗

Purification and properties of L-asparaginase EC-2 from Escherichia coli 055:B5.

1. L-Asparaginase has been isolated from aerobically grown Escherichia coli 055:B5 and purified about 140-fold in a three-step procedure involving acidification to pH 4.5, ammonium sulphate fractionation and column chromatography on DEAE-Sephadex A-50. The activity of the preparation is 140 U/mg protein. 2. The enzyme acts within a broad pH range (pH 5-9) and is affected neither by PCMB, N-ethylmaleimide nor metal ions. 3. Molecular weight of the isolated asparaginase is 130 000.

Asparaginase↗