Influence of Blastocystis hominis on the small intestine and lactase enzyme activity

2021 ◽  
Author(s):  
Gehad A. Basuony ◽  
Maha M.A.Basyoni ◽  
Mohamed Sherif Ismail Negm ◽  
Eman Ali Mohamed Mostafa ◽  
Eman Sayed El-Wakil ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Small Intestine ◽  
Blastocystis Hominis

Ornithine decarboxylase in rat small intestine: stimulation with food or insulin

1976 ◽  
Vol 231 (5) ◽  
pp. 1557-1561 ◽  
Author(s):  
DV Maudsley ◽  
J Leif ◽  
Y Kobayashi
Keyword(s):  
Enzyme Activity ◽  
Small Intestine ◽  
Ornithine Decarboxylase ◽  
Diamine Oxidase ◽  
Actinomycin D ◽  
Histidine Decarboxylase ◽  
Decarboxylase Activity ◽  
Adenosylmethionine Decarboxylase ◽  
Diamine Oxidase Activity ◽  
Similarities And Differences

Ornithine decarboxylase in the small intestine of starved rats was stimulated 3- to 10-fold by refeeding or administration of insulin. A peak is observed 3-5 h following treatment after which the enzyme activity rapidly declines. The rise in ornithine decarboxylase is reduced by actinomycin D or cycloheximide. The increase in enzyme activity occurs mainly in the duodenum and jejunum with less than a twofold change being observed in the ileum. A small (twofold) increase in S-adenosylmethionine decarboxylase activity in the small intestine was observed after food, but there was no change in diamine oxidase activity. Whereas pentagastrin and metiamide administration markedly stimulated histidine decarbosylase in the gastric mucosa, no consistent effect of these agents on ornithine decarboxylase in the small intestine was observed. The similarities and differences between histidine decarboxylase and ornithine decarboxylase are discussed.

Development and tissue distribution of sucrase-isomaltase mRNA in rats

1990 ◽  
Vol 258 (1) ◽  
pp. G52-G58 ◽  
Author(s):  
L. L. Leeper ◽  
S. J. Henning
Keyword(s):  
Enzyme Activity ◽  
Small Intestine ◽  
Northern Blot ◽  
Blot Analysis ◽  
Molecular Basis ◽  
Northern Blot Analysis ◽  
Sucrase Activity ◽  
Old Rats ◽  
Two Parameters ◽  
Precocious Development

Previous studies of sucrase-isomaltase (SI) activities have shown this complex to be absent in the suckling rat and to appear during the weaning period. We describe here the cloning of a heterologous SI cDNA and its use for the quantitation of SI mRNA as a first step toward understanding the molecular basis of SI development. A survey of RNA from 12 tissues of mature rats by Northern blot analysis showed a 6-kb band of SI mRNA only in the small intestine. Within the latter, both sucrase activity and SI mRNA peaked in the jejunum. Assay of jejunal tissue from developing rats showed sucrase activity and SI mRNA to be first detectable at 18 days, to rise in parallel through 24 days, and then to diverge a little (enzyme activity being lower) by 36 days. When glucocorticoid was administered to 10-day-old rats, neither sucrase activity nor SI mRNA was detectable 12 h later. Both parameters were readily detected 24 h postinjection, although the mRNA had risen relatively more than the enzyme activity. The two parameters increased in concert through 5 days postinjection and then plateaued. We conclude that, with respect to distribution along the intestine and to normal and precocious development, activities of SI in the rat are determined primarily by the abundance of its mRNA.

The Expression of Enzyme Activity of Biopsy Tissue from the Small Intestine

Digestion ◽  
1977 ◽  
Vol 15 (3) ◽  
pp. 182-187 ◽  
Author(s):  
B.B. Scott ◽  
M.J. Fairman ◽  
C. Toothill ◽  
M.S. Losowsky
Keyword(s):  
Enzyme Activity ◽  
Small Intestine ◽  
Biopsy Tissue

scholarly journals The influence of inclusion of either an antibiotic or a probiotic in the diet on the development of digestive enzyme activity in the pig

1990 ◽  
Vol 64 (1) ◽  
pp. 59-70 ◽  
Author(s):  
G. K. Collington ◽  
D. S. Parker ◽  
D. G. Armstrong
Keyword(s):  
Enzyme Activity ◽  
Small Intestine ◽  
Treatment Group ◽  
Present Experiment ◽  
Digestive Enzyme ◽  
Digestive Enzyme Activity ◽  
Growth Promoter ◽  
Peptidase Activity ◽  
Creep Feed

The aim of the present experiment was to determine the influence of either probiotic or antibiotic inclusion in the diets of pigs from birth on the development of enzyme activity in the small intestine. Pigs were fed on creep feed and grower diets containing either a probiotic, an antibiotic or no added growth promoter. At 7, 17, 42 and 80 d of age pigs from each treatment group were sampled to investigate the development of carbohydrase and peptidase activity in the mucosa at five sites along the small intestine. Inclusion of either the probiotic or antibiotic had a significant effect on the development of sucrase (sucrose α-D-glucohydrolase;EC3.2.1.48), lactase (β-D-galactoside galactohydrolase;EC3.2.1.23) and tripeptidase (EC3.4.11.4) activities before weaning but had no effect on depeptidase (EC3.14.13.11) activity. The study of the distribution of enzyme activity along the small intestine showed significant differences between the proximal and distal sections associated with weaning.

Catabolism of plasma enzymes, as studied with 125I-labeled lactate dehydrogenase-1 in the rabbit.

1976 ◽  
Vol 22 (8) ◽  
pp. 1269-1276
Author(s):  
J H Wilkinson ◽  
A R Qureshi
Keyword(s):  
Enzyme Activity ◽  
Small Intestine ◽  
Catalytic Activity ◽  
Lactate Dehydrogenase ◽  
Extracellular Fluid ◽  
Second Phase ◽  
Enzyme Protein ◽  
Plasma Enzymes ◽  
Close Proximity ◽  
Intestinal Contents

Abstract Circulating enzymes may be inactivated in the plasma and the inactive breakdown products may be hydrolyzed in the lumen of the small intestine. Evidence for this mechanism was based upon previous studies with 125I-labeled lactate dehydrogenase-5, and here similar studies with radioiodinated lactate dehydrogenase-1 are reported, to determine whether this isoenzyme is similarly catabolized. The pure rabbit enzyme was labeled with 125I by use of lactoperoxidase and hydrogen peroxide (the labeled enzyme had 80-85% of the original catalytic activity). After its intravenous injection into rabbits, plasma enzyme activity and radioactivity disappeared during the first 4 h at similar fast rates, apparently because of distribution of the injected enzyme throughout the extracellular fluid. During a second phase (30-h), catalytic activity disappeared significantly faster than radioactivity, suggesting inactivation of the enzyme in either the plasma or a compartment in close proximity to it, or both. Enzyme activity then remained constant while plasma radioactivity continued to decrease at a slower, exponential rate, apparently owing to removal of breakdown products. In no case did tissue radioactivity, studied 6 h after injection, approach that of plasma. We therefore conclude that removal of the enzyme protein or its breakdown products is a passive process. Appreciable radioactivity was detected in the intestinal contents, a finding which suggests that removal via the small intestine is an important route for the removal of inactivated enzyme products from the circulation. Less than 3% of the injected radioactivity appeared in the feces during the first three days; urinary excretion accounted for about 67% during the same period, about 60% of which consisted of radio-iodinated amino-acids, the remainder of iodide. Free mono- and di-iodotyrosines were among the products excreted. These appear to originate from absorption of the products of further breakdown of the enzyme molecule in the intestine.

The influence of inclusion of a probiotic in the diet on the development of enzyme activity in the small intestine of the pig

1990 ◽  
Vol 1990 ◽  
pp. 97-97
Author(s):  
G.K. Collington ◽  
D.S. Parker ◽  
D.G. Armstrong ◽  
M. Ellis
Keyword(s):  
Enzyme Activity ◽  
Small Intestine ◽  
Brush Border ◽  
Microbial Population ◽  
Hydrolase Activity ◽  
Before And After ◽  
Probiotic Preparation

The objective of the present study was to investigate the development of hydrolase enzyme activity at six sites along the small intestine of the pig before and after weaning and the influence inclusion of a probiotic preparation had upon this. The enzymes studied lactase, dipeptidase and tripeptidase are primarily associated with the brush border of the enterocyte cell and expression of hydrolase activity has been shown to be affected by manipulation of the microbial population of the gut.

scholarly journals Artificial rearing of pigs

1970 ◽  
Vol 24 (3) ◽  
pp. 827-842 ◽  
Author(s):  
R. Braude ◽  
M.J. Newport ◽  
J.W. Porter
Keyword(s):  
Enzyme Activity ◽  
Small Intestine ◽  
Proteolytic Enzyme ◽  
Time Course ◽  
Stomach Contents ◽  
Stomach Wall ◽  
Starvation Period ◽  
Artificial Rearing ◽  
Proteolytic Enzyme Activity ◽  
Marked Decline

1. The time course of digestion of milk protein was studied in the 28-d-old pig given a test meal of homogenized cow's milk after a preliminary starvation period.2. The milk was found to clot in the stomach 15–30 min after the meal. The soluble or ‘whey’ fraction of the stomach contents rapidly passed into the small intestine. Most of the clotted digesta had also left the stomach z h after the meal.3. The distribution of digesta was studied in six equal segments of the small intestine. In general, there were no significant increases in the amount of intestinal contents at any time after the meal when compared with those in starved pigs, suggesting that digestion of milk at this age is a very efficient process.4. Fractionation of the soluble digesta from the stomach and small intestine in Sephadex G-25 indicated that relatively little proteolysis occurred in the stomach, but in the small intestine digestion proceeded rapidly, producing a considerable increase in free amino acids in the mid-region.5. The level of proteolytic enzyme activity in the stomach wall was elevated at 15 min after the meal, but thereafter returned rapidly to the prefeeding levels. Increasing the level of feeding increased the enzyme activity of the digesta and stomach wall. The enzyme activity appeared to be mainly adsorbed by the stomach clot.6. The proteolytic enzyme activity in the pancreas was unaffected by the meal. However, the activity in the contents of the small intestine increased after the meal, reaching a maximum value at 45 min. Some accumulation of enzymes was found in the lower part of the small intestine, except in the region of the distal ileum where a marked decline in enzyme activity occurred. Increasing the level of feeding increased the proteolytic enzyme activity in the contents of the small intestine.7. The soluble marker polyethylene glycol was not entirely satisfactory as an indicator of the rate of passage of digesta. The concentration of the marker was found to be greater in the soluble stomach fraction than in the clot shortly after the milk had been ingested. The transit time of the marker from ingestion to the terminal ileum was 2–3 h.

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