Andrographolide and kalmegh (Andrographis paniculata) extract: effect on intestinal brush-border membrane-bound hydrolases. 1985

B R Choudhury, and M K Poddar

Oral (p.o.) administration of a single dose of kalmegh leaf extract (KE; 0.5 g/kg and 1.0 g/kg) or andrographolide (A; 5 mg/kg and 10 mg/kg) to adult male albino rats (100-120 g) produced a dose-related and time-dependent characteristic activation of brush-border membrane-bound hydrolases, viz. lactase, maltase and sucrase in three regions of small intestine (viz. duodenum, jejunum and ileum). The maximum stimulation of these disaccharidases was obtained at 6 hr of either KE or A administration. Further, it was also noted that the extent of activation of the disaccharidases with KE or A, both at higher and lower doses, followed the order: (a) Maltase greater than sucrase greater than lactase in duodenum and (b) Maltase greater than lactase greater than sucrase in jejunum and ileum. Long term administration (for 7, 15 and 30 consecutive days) of either KE (500 p.o.) or A (5 mg/kg/day; p.o.) stimulated lactase, maltase and sucrase in all parts of the small intestine. Maximum stimulation of lactase and maltase was noted after 30 consecutive days of treatment while sucrase exhibited maximum activation after 15 consecutive of treatment with either KE or A. These results suggest that both KE and A accelerate intestinal digestion and absorption of carbohydrate by activating these intestinal disaccharidases.

UI MeSH Term Description Entries
D007421 Intestine, Small The portion of the GASTROINTESTINAL TRACT between the PYLORUS of the STOMACH and the ILEOCECAL VALVE of the LARGE INTESTINE. It is divisible into three portions: the DUODENUM, the JEJUNUM, and the ILEUM. Small Intestine,Intestines, Small,Small Intestines
D008297 Male Males
D008871 Microvilli Minute projections of cell membranes which greatly increase the surface area of the cell. Brush Border,Striated Border,Border, Brush,Border, Striated,Borders, Brush,Borders, Striated,Brush Borders,Microvillus,Striated Borders
D009284 Naphthols Naphthalene derivatives carrying one or more hydroxyl (-OH) groups at any ring position. They are often used in dyes and pigments, as antioxidants for rubber, fats, and oils, as insecticides, in pharmaceuticals, and in numerous other applications. Hydroxynaphthalene,Hydroxynaphthalenes,Naphthol
D010936 Plant Extracts Concentrated pharmaceutical preparations of plants obtained by removing active constituents with a suitable solvent, which is evaporated away, and adjusting the residue to a prescribed standard. Herbal Medicines,Plant Extract,Extract, Plant,Extracts, Plant,Medicines, Herbal
D010946 Plants, Medicinal Plants whose roots, leaves, seeds, bark, or other constituent parts possess therapeutic, tonic, purgative, curative or other pharmacologic attributes, when administered to man or animals. Herbs, Medicinal,Medicinal Herbs,Healing Plants,Medicinal Plants,Pharmaceutical Plants,Healing Plant,Herb, Medicinal,Medicinal Herb,Medicinal Plant,Pharmaceutical Plant,Plant, Healing,Plant, Medicinal,Plant, Pharmaceutical,Plants, Healing,Plants, Pharmaceutical
D004224 Diterpenes Twenty-carbon compounds derived from MEVALONIC ACID or deoxyxylulose phosphate. Diterpene,Diterpenes, Cembrane,Diterpenes, Labdane,Diterpenoid,Labdane Diterpene,Norditerpene,Norditerpenes,Norditerpenoid,Cembranes,Diterpenoids,Labdanes,Norditerpenoids,Cembrane Diterpenes,Diterpene, Labdane,Labdane Diterpenes
D004789 Enzyme Activation Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme. Activation, Enzyme,Activations, Enzyme,Enzyme Activations
D006867 Hydrolases Any member of the class of enzymes that catalyze the cleavage of the substrate and the addition of water to the resulting molecules, e.g., ESTERASES, glycosidases (GLYCOSIDE HYDROLASES), lipases, NUCLEOTIDASES, peptidases (PEPTIDE HYDROLASES), and phosphatases (PHOSPHORIC MONOESTER HYDROLASES). EC 3. Hydrolase
D000520 alpha-Glucosidases Enzymes that catalyze the exohydrolysis of 1,4-alpha-glucosidic linkages with release of alpha-glucose. Deficiency of alpha-1,4-glucosidase may cause GLYCOGEN STORAGE DISEASE TYPE II. Acid Maltase,Lysosomal alpha-Glucosidase,Maltase,Maltases,Maltase-Glucoamylase,Neutral Maltase,Neutral alpha-Glucosidase,alpha-Glucosidase,Lysosomal alpha Glucosidase,Maltase Glucoamylase,Neutral alpha Glucosidase,alpha Glucosidase,alpha Glucosidases,alpha-Glucosidase, Lysosomal,alpha-Glucosidase, Neutral

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