Pepsin and its multiple forms in early life.
Pepsin and its multiple molecular forms have been studied in pre-term and post-term Nigerian infants. The levels of total enzyme activity and acidity were lower in the pre-term infants when compared to term and post-term infants. Resolutions of the various species by ion-exchange chromatography and electrophoresis revealed that the development of specific isoenzymes in term infants occurred towards the end of the neonatal period. Differential development of the enzyme and the isoenzyme in the neonatal period may have important clinical bearing on the subsequent pancreatic protease hydrolysis which may provide a basis for evaluating gastric capacity for nutritional management of these infants.
D002712:Chlorides / Q000032:analysis; D002852:Chromatography, Ion Exchange; D005260:Female; D006801:Humans; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D007231:Infant, Newborn / Q000378:metabolism*; D007233:Infant, Postmature / Q000378:metabolism*; D007234:Infant, Premature / Q000378:metabolism*; D007527:Isoenzymes / Q000378:metabolism*; D008297:Male; D010434:Pepsin A / Q000378:metabolism*; D011188:Potassium / Q000032:analysis; D012964:Sodium / Q000032:analysis; D013270:Stomach / Q000201:enzymology*
D002712:Chlorides; D007527:Isoenzymes; D012964:Sodium; D010434:Pepsin A; D011188:Potassium