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| Duarte,Silvana; Paiva,Marco A. R.; Lara,Camila C.; Bemquerer,Marcelo P.; Araújo,Francisco Gerson. |
| The enzymatic activities involved in the digestion of proteins and carbohydrates were compared among three organs of the digestive track of two Siluriformes fish species, and between two areas: a reservoir, and an area downriver of it. Our aim was to test the hypothesis that the digestive organs of species with varied feeding habits have different enzymatic activities, and that the enzymatic activity differs among seasons and environmental conditions. The iliophagous/herbivorous species Hypostomus auroguttatus Kner, 1854 had higher trypsin-like, chymotrypsin-like peptidase and β-glucosidase activity in the intestine when compared with the omnivorous species Pimelodus maculatus Lacepède, 1803, whereas the latter had more hepatic trypsin-like activity than... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Enzymatic activity; Fishes; Physiology; Reservoirs; Siluriformes; Peptidases; Β-glucosidase. |
| Ano: 2013 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1984-46702013000300006 |
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| We have studied the metabolism of diglycine and triglycine in the isolated non-filtering rat kidney. Kidneys from adult male Wistar Kyoto rats weighing 250-350 g were perfused with Krebs-Henseleit solution containing either 1 mM diglycine or triglycine. The analysis of the peptide residues and their components was performed using an amino acid microanalyzer utilizing ion exchange chromatography. Diglycine was degraded to a final concentration of 0.09 mM after 120 min (91%); this degradation occurred predominantly during the first hour, with a 56% reduction of the initial concentration. The metabolism of triglycine occurred similarly, with a final concentration of 0.18 mM (82%); during the first hour there was a 67% reduction of the initial concentration of... |
| Tipo: Info:eu-repo/semantics/other |
Palavras-chave: Non-filtering kidney; Dipeptide; Tripeptide; Metabolism; Peptidases. |
| Ano: 1997 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X1997000200005 |
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