Sucrase-alpha-dextrinase in the rat. Postinsertional conversion to inactive molecular species by a carbohydrate-free diet.

Quan, Richard; Gray, Gary M.

doi:10.1172/jci116520

Cited by 6 publications

(5 citation statements)

References 25 publications

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“…A similar relationship among the specific activities of these enzymes has been reported previously (Thomsen and Tasman-Jones, 1982;Carmona et al, 1996). The sucrase to maltase activity ratio was 0.95; this value is slightly lower than the 1.2 reported by Quan and Gray (1993). Lactase activity was one order of magnitude smaller in comparison with sucrase and maltase.…”

Section: Dietary Fibersupporting

confidence: 87%

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Effect of legume dietary fiber on rat disaccharidase activity in vitro

Infante

García

Rivera

2008

Nutrition &Amp; Food Science

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Purpose -Brush border intestinal disaccharidases (maltase, sucrase and lactase) play an important role in carbohydrate assimilation. These enzymes are located on the brush border and may interact with legume seed components such as dietary fiber and polyphenols. The purpose of this paper is to assess the effect of legume dietary fiber on rat disaccharidase in vitro. Design/methodology/approach -Rat intestinal disaccharidases from Sprague-Dawley rats fed a basal diet for 21 days were partially purified from intestinal scrapings. Enzyme activities were tested in vitro in the absence and presence of total dietary fiber isolated from Phaseolus vulgaris (Varieties Tacarigua and Montalbán) and Vigna unguiculata (Varieties Unare and Tuy) seeds that differ in fiber and polyphenol content. Dietary fiber was purified using the AOAC method. Findings -The specific activities of the intestinal brush-border disaccharidases from rats fed the basal diet were 3.29 ± 0.06, 3.13 ± 0.62 and 0.18 ± 0.04 mmoles of glucose released/mg of protein/min for maltase, sucrase and lactase, respectively. Total dietary fiber from the legume tested inhibited both sucrase and maltase. Fiber from the four seeds tested affected sucrase similarly (average inhibition 35 per cent) whereas the fiber residue from P. vulgaris Montalbán was more effective on maltase (26.7 per cent) than that from P. vulgaris Tacarigua (12.2 per cent). Effect of V. unguiculata fibers on maltase was similar and somewhat in between those from P. vulgaris. Originality/value -These results suggest that dietary fiber, as well as other factors from beans with antiphysiological effect, such as condensed tannins and fitic acid possibly associated with the dietary fiber, may impair carbohydrate availability and may contribute to the low glycemic index proper of these foodstuffs.

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Section: Dietary Fibersupporting

confidence: 87%

“…Lactase activity was one order of magnitude smaller in comparison with sucrase and maltase. This is due to the fact that the basal diet did not contain lactose to induce higher lactose levels (Quan and Gray, 1993). These results were obtained from experiments in vivo; in vitro experiments were not carried out in these studies.…”

Section: Dietary Fibermentioning

confidence: 99%

Effect of legume dietary fiber on rat disaccharidase activity in vitro

Infante

García

Rivera

2008

Nutrition &Amp; Food Science

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“…Sabat and coworkers argued that the increase in activity of these two brush border carbohydrases represents a nonspecific response to the high-protein diet. Conversely, Quan and Gray (1993) found that rats decrease the amount of active sites per enzyme molecule for isomaltase, thereby decreasing their disaccharidase activity in the absence of substrate. Overall, the diverse patterns of maltase and isomaltase activities among the pricklebacks on the high-protein, low-starch diet are not different from those reported for birds and other fishes fed high-versus low-starch diets (Kawai and Ikeda 1972;Buddington and Hilton 1987;Levey et al 1999;Caviedes-Vidal et al 2000), but they expose our uncertainty about the mechanisms underlying why some animals modulate digestive enzyme activities whereas others do not.…”

Section: Discussionmentioning

confidence: 92%

Digestive Enzyme Activities in Herbivorous and Carnivorous Prickleback Fishes (Teleostei: Stichaeidae): Ontogenetic, Dietary, and Phylogenetic Effects

German

Horn

Gawlicka

2004

Physiological and Biochemical Zoology

180

147

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We measured the activities of eight digestive enzymes in four species of herbivorous and carnivorous prickleback fishes and determined the effects of ontogeny, diet, and phylogeny on these enzyme activities. Of the four species, Cebidichthys violaceus and Xiphister mucosus shift to a more herbivorous diet as they grow (> or =45 mm SL [standard length]), whereas Xiphister atropurpureus and Anoplarchus purpurescens remain carnivores throughout life. Digestive enzyme activities of small (30-40 mm SL) carnivorous juveniles were compared with those of larger (60-75 mm SL) wild-caught juveniles that had consumed a natural diet and larger (60-75 mm SL) juveniles raised on a high-protein animal diet. Cebidichthys violaceus and both species of Xiphister showed ontogenetic changes in digestive enzyme activities, whereas A. purpurescens did not. Despite dietary differences between X. atropurpureus and X. mucosus, these sister taxa displayed the most similar digestive enzyme activities from ontogenetic and dietary perspectives (high alpha-amylase and lipase and low trypsin and aminopeptidase activities), and both were more similar to C. violaceus, a member of the same largely herbivorous clade, than either was to A. purpurescens, a member of an adjacent, carnivorous clade. The results support the hypothesis that phylogeny influences digestive enzyme activities in these fishes. Anoplarchus purpurescens, a carnivore with a diverse diet, showed great plasticity in enzyme activity, especially trypsin and aminopeptidase, which were elevated in this species to the highest level among the four species after consuming the high-protein diet. These results support the hypothesis that fishes with relatively broad diets can modulate digestive enzyme activities in response to changes in dietary composition.

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“…14 SI consists of two subunits, sucrase and isomaltase, which are cleaved by luminal proteases but remain associated through noncovalent interactions. 15 The sucrase subunit has both maltase (α-1,4) and sucrase (α-1,2) activities, while the isomaltase subunit has maltase (α-1,4) and isomaltase (α-1,6) activities. 16 SI is therefore involved in the digestion of both sugars and starch.…”

Section: Introductionmentioning

confidence: 99%

“…Sucrase isomaltase (SI) is a highly N - and O -glycosylated brush border type-II membrane protein with various α-glucosidase activities and is trafficked to the cell surface through association with lipid rafts . SI consists of two subunits, sucrase and isomaltase, which are cleaved by luminal proteases but remain associated through noncovalent interactions . The sucrase subunit has both maltase (α-1,4) and sucrase (α-1,2) activities, while the isomaltase subunit has maltase (α-1,4) and isomaltase (α-1,6) activities .…”

Section: Introductionmentioning

confidence: 99%