Separation and characterization of intestinal brush border enzymes in adult rats and in suckling rats under normal conditions and after hydrocortisone injections.
Adult and suckling (13 days old) rat intestinal brush borders have been purified by the procedure of Schmitz et al. (25). Enzymatic proteins have been separated by polyacrylamide gel electrophoresis. In the adult rat, enzyme proteins have been separated by polyacrylamide gel electrophoresis. In the adult rat, enzyme activities in order from the origin were: maltase/glucoamylase/sucrase-isomaltase (protein band 3), lactase (protein band 5), maltase/sucrase-isomaltase (protein band 6) and alkaline phosphatase (protein bands 8 and 9). In the suckling rat, protein band 5 associated with lactase activity was found to be markedly higher compared to the adult rat. Gels were completely devoid of sucrase-isomaltase activity while protein band 3 was strikingly reduced and protein band 6 absent. After hydrocortisone administration to suckling rats, a new band associated with sucrase-isomaltase activity appeared in position 6, whereas protein band 3 markedly increased with the simultaneous appearance of sucrase-isomaltase activity.
D000375:Aging; D000469:Alkaline Phosphatase / Q000302:isolation & purification / Q000378:metabolism; D000818:Animals; D000831:Animals, Newborn / Q000378:metabolism*; D004186:Disaccharidases / Q000302:isolation & purification / Q000378:metabolism; D006854:Hydrocortisone / Q000494:pharmacology*; D007413:Intestinal Mucosa / Q000201:enzymology*; D008871:Microvilli / Q000201:enzymology; D051381:Rats
D000469:Alkaline Phosphatase; D004186:Disaccharidases; D006854:Hydrocortisone