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4.
Ross Fiziol Zh Im I M Sechenova ; 83(11-12): 151-7, 1997.
Artículo en Ruso | MEDLINE | ID: mdl-9541967

RESUMEN

Daily perfusion of the pig small intestine with the sodium nitrate solution entailed a 2-3-fold drop in absorption of glucose and 1.5-2.0-fold drop in absorption of glycine. The sodium nitrate solution being substituted with saline, the absorption of both substances recovered by approximately 80%. The toxic effect of sodium nitrate seems to be due to both the local effect upon the small intestine mucosa and the general effect upon the organism.


Asunto(s)
Glucosa/metabolismo , Glicina/metabolismo , Absorción Intestinal/efectos de los fármacos , Intestino Delgado/efectos de los fármacos , Nitratos/toxicidad , Animales , Mucosa Intestinal/efectos de los fármacos , Mucosa Intestinal/metabolismo , Intestino Delgado/metabolismo , Perfusión , Porcinos
5.
Br J Nutr ; 34(2): 205-20, 1975 Sep.
Artículo en Inglés | MEDLINE | ID: mdl-1174495

RESUMEN

1. The hydrolysis of glycyl-L-leucine, glycyl-L-tyrosine, tributyrin, sucrose, maltose, soluble starch and alpha- and beta-glycerophosphates by everted segments of rat intestine was estimated separately or in combination. 2. A comparative study showed significant interaction between different substrates which affected their digestion. 3. Two types of interaction were identified: products of hydrolysis (1) affected the hydrolysis of homologous substances, e.g. methionine and alanine inhibited glycyl-L-leucine hydrolysis, maltose reduced glucoamylase (alpha-1,4-glucan glucohydrolase; EC 3-2-1-3) activity (intracatenary interactions); (2) interfered with the hydrolysis of a different group of substances, e.g. tributyrin inhibited dipeptidase (glycyl-L-leucine hydrolase; EC 3-4-3-2) and alkaline phosphatase (EC 3-1-3-1), glycyl-L-leucine interfered with the activity of the latter enzyme (intercatenary interactions). 4. Mechanisms of interactions were suggested by the results of a comparison of the extent of inhibition or activation of two enzymes (glycyl-L-leucine hydrolase and alkaline phosphatase) in situ in everted intestinal segments or after solubilization with papain or Triton X-100, and different treatments known to affect allosteric sites of these enzymes. 5. Tributyrin and dipeptides were found to act on alkaline phosphatase as allosteric regulators. A discontinuity of the Arrhenius plot suggested the existence of different enzyme conformations which were re-arranged by tributyrin. 6. Substrate interactions in digestion were found in adult rat, cat, rabbit and hen. Substantial differences were found between classes (Aves and Mammalia), orders (rodents, lagomorphs and carnivores) and between age-groups within an animal strain (in this instance, for the rat). 7. These interactions are thought to be involved in the co-ordination of digestion with intestinal absorption and to regulate the time and site of subsequent hydrolysis.


Asunto(s)
Mucosa Intestinal/metabolismo , Intestino Delgado/fisiología , Fosfatasa Alcalina/antagonistas & inhibidores , Fosfatasa Alcalina/metabolismo , Regulación Alostérica , Animales , Transporte Biológico , Gatos , Pollos , Digestión , Dipeptidasas/antagonistas & inhibidores , Dipeptidasas/metabolismo , Activación Enzimática , Glucosidasas/antagonistas & inhibidores , Glucosidasas/metabolismo , Absorción Intestinal , Lipasa/metabolismo , Conejos , Ratas , Especificidad de la Especie
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