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Similarity of hydrolyzing activity of human and rat small intestinal disaccharidases

BACKGROUND: The purpose of this study was to clarify whether it is possible to extrapolate results from studies of the hydrolyzing activity of disaccharidases from rats to humans. MATERIALS AND METHODS: We measured disaccharidase activity in humans and rats using identical preparation and assay meth...

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Autores principales: Oku, Tsuneyuki, Tanabe, Kenichi, Ogawa, Shigeharu, Sadamori, Naoki, Nakamura, Sadako
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Dove Medical Press 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3163924/
https://www.ncbi.nlm.nih.gov/pubmed/21904461
http://dx.doi.org/10.2147/CEG.S19961
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author Oku, Tsuneyuki
Tanabe, Kenichi
Ogawa, Shigeharu
Sadamori, Naoki
Nakamura, Sadako
author_facet Oku, Tsuneyuki
Tanabe, Kenichi
Ogawa, Shigeharu
Sadamori, Naoki
Nakamura, Sadako
author_sort Oku, Tsuneyuki
collection PubMed
description BACKGROUND: The purpose of this study was to clarify whether it is possible to extrapolate results from studies of the hydrolyzing activity of disaccharidases from rats to humans. MATERIALS AND METHODS: We measured disaccharidase activity in humans and rats using identical preparation and assay methods, and investigated the similarity in hydrolyzing activity. Small intestinal samples without malignancy were donated by five patients who had undergone bladder tumor surgery, and homogenates were prepared to measure disaccharidase activity. Adult rat homogenates were prepared using small intestine. RESULTS: Maltase activity was the highest among the five disaccharidases, followed by sucrase and then palatinase in humans and rats. Trehalase activity was slightly lower than that of palatinase in humans and was similar to that of sucrase in rats. Lactase activity was the lowest in humans, but was similar to that of palatinase in rats. Thus, the hydrolyzing activity of five disaccharidases was generally similar in humans and rats. The relative activity of sucrose and palatinase versus maltase was generally similar between humans and rats. The ratio of rat to human hydrolyzing activity of maltase, sucrase, and palatinase was 1.9–3.1, but this was not a significant difference. Leaf extract from Morus alba strongly inhibited the activity of maltase, sucrase, and palatinase, but not trehalase and lactase, and the degree of inhibition was similar in humans and rats. L-arabinose mildly inhibited sucrase activity, but hardly inhibited the activity of maltase, palatinase, trehalase and lactase in humans and rats. The digestibility of 1-kestose, galactosylsucrose, and panose by small intestinal enzymes was very similar between humans and rats. CONCLUSION: These results demonstrate that the digestibility of newly developed saccharide materials evaluated by rat small intestinal enzymes can substitute for evaluation using human enzymes.
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spelling pubmed-31639242011-09-08 Similarity of hydrolyzing activity of human and rat small intestinal disaccharidases Oku, Tsuneyuki Tanabe, Kenichi Ogawa, Shigeharu Sadamori, Naoki Nakamura, Sadako Clin Exp Gastroenterol Original Research BACKGROUND: The purpose of this study was to clarify whether it is possible to extrapolate results from studies of the hydrolyzing activity of disaccharidases from rats to humans. MATERIALS AND METHODS: We measured disaccharidase activity in humans and rats using identical preparation and assay methods, and investigated the similarity in hydrolyzing activity. Small intestinal samples without malignancy were donated by five patients who had undergone bladder tumor surgery, and homogenates were prepared to measure disaccharidase activity. Adult rat homogenates were prepared using small intestine. RESULTS: Maltase activity was the highest among the five disaccharidases, followed by sucrase and then palatinase in humans and rats. Trehalase activity was slightly lower than that of palatinase in humans and was similar to that of sucrase in rats. Lactase activity was the lowest in humans, but was similar to that of palatinase in rats. Thus, the hydrolyzing activity of five disaccharidases was generally similar in humans and rats. The relative activity of sucrose and palatinase versus maltase was generally similar between humans and rats. The ratio of rat to human hydrolyzing activity of maltase, sucrase, and palatinase was 1.9–3.1, but this was not a significant difference. Leaf extract from Morus alba strongly inhibited the activity of maltase, sucrase, and palatinase, but not trehalase and lactase, and the degree of inhibition was similar in humans and rats. L-arabinose mildly inhibited sucrase activity, but hardly inhibited the activity of maltase, palatinase, trehalase and lactase in humans and rats. The digestibility of 1-kestose, galactosylsucrose, and panose by small intestinal enzymes was very similar between humans and rats. CONCLUSION: These results demonstrate that the digestibility of newly developed saccharide materials evaluated by rat small intestinal enzymes can substitute for evaluation using human enzymes. Dove Medical Press 2011-06-27 /pmc/articles/PMC3163924/ /pubmed/21904461 http://dx.doi.org/10.2147/CEG.S19961 Text en © 2011 Oku et al, publisher and licensee Dove Medical Press Ltd. This is an Open Access article which permits unrestricted noncommercial use, provided the original work is properly cited.
spellingShingle Original Research
Oku, Tsuneyuki
Tanabe, Kenichi
Ogawa, Shigeharu
Sadamori, Naoki
Nakamura, Sadako
Similarity of hydrolyzing activity of human and rat small intestinal disaccharidases
title Similarity of hydrolyzing activity of human and rat small intestinal disaccharidases
title_full Similarity of hydrolyzing activity of human and rat small intestinal disaccharidases
title_fullStr Similarity of hydrolyzing activity of human and rat small intestinal disaccharidases
title_full_unstemmed Similarity of hydrolyzing activity of human and rat small intestinal disaccharidases
title_short Similarity of hydrolyzing activity of human and rat small intestinal disaccharidases
title_sort similarity of hydrolyzing activity of human and rat small intestinal disaccharidases
topic Original Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3163924/
https://www.ncbi.nlm.nih.gov/pubmed/21904461
http://dx.doi.org/10.2147/CEG.S19961
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