scholarly journals LYSOSOMAL ENZYMES OF RAT INTESTINAL MUCOSA

1964 ◽  
Vol 23 (2) ◽  
pp. 233-240 ◽  
Author(s):  
Lichu Hsu ◽  
A. L. Tappel
Keyword(s):  
Rat Liver ◽  
Intestinal Mucosa ◽  
Digestive Enzymes ◽  
Lysosomal Enzymes ◽  
Liver Enzymes ◽  
Enzyme Release ◽  
Centrifugal Forces ◽  
Physiological Functions ◽  
Specific Activities

Six intracellular hydrolases known to be associated with lysosomes in rat liver were found in rat intestinal mucosa. The extent to which they were particulate-bound and the degree of enzyme release when the particulate fractions were suspended in hypotonic media followed the same pattern in both mucosa and liver. The specific activities of the mucosa enzymes were either comparable to or slightly smaller than those of the liver enzymes. These results suggest that the mucosa hydrolases belong to lysosome-like particles. However, differential fractionation of the mucosa indicated that the particles from the mucosa sediment at lower centrifugal forces than do those from the liver and are more heterogeneous in size, bearing a closer resemblance to kidney lysosomes. Possible physiological functions of particulate-bound digestive enzymes in intestinal mucosa are discussed.

scholarly journals Studies on mammalian glucoamylases with special reference to monkey intestinal glucoamylase

1970 ◽  
Vol 117 (5) ◽  
pp. 939-946 ◽  
Author(s):  
B. Seetharam ◽  
N. Swaminathan ◽  
A. N. Radhakrishnan
Keyword(s):  
Special Reference ◽  
Enrichment Factor ◽  
Intestinal Mucosa ◽  
Liver Enzymes ◽  
Gel Filtration ◽  
Maximum Activity ◽  
Similar Magnitude ◽  
Glucoamylase Activity ◽  
Specific Activities ◽  
Intestinal Enzyme

1. Highly purified preparations of glucoamylase were obtained from liver, spleen and intestine of the monkey. The enrichment factor was lower for intestine (60-fold) compared with that of liver (1200-fold) and of spleen (2000-fold) but the final specific activities were of a similar magnitude. 2. The liver and spleen enzymes had maximum activity at pH4.8 whereas the intestinal enzyme showed an optimum at pH5.8. The Km values for both starch and maltose with spleen and liver enzymes were higher than for the intestinal enzyme. With the intestinal enzyme, the Vmax. values were higher for both starch and maltose than those of the spleen and liver enzymes. 3. Gel filtration on Sephadex G-200 under identical conditions revealed that liver and spleen enzymes emerge from the columns much later than the intestinal enzyme. 4. Evidence is presented that the glucoamylase activity of the intestinal mucosa is exhibited by the maltase II fraction. 5. Tris, pentaerythritol and turanose inhibited glucoamylase from all the three tissues, but turanose inhibited the spleen and liver enzymes to a higher degree than the intestinal enzyme.

The Effect of Cortisone Acetate on Lysosomal Enzyme Levels In Rat Liver

1972 ◽  
Vol 50 (1) ◽  
pp. 20-24 ◽  
Author(s):  
A. Kyaw ◽  
A. Mellors
Keyword(s):  
Acid Phosphatase ◽  
Rat Liver ◽  
Lysosomal Enzyme ◽  
Lysosomal Enzymes ◽  
Specific Activity ◽  
Cortisone Acetate ◽  
Maximum Increase ◽  
Tyrosine Transaminase ◽  
Specific Activities

Increases in the levels of four lysosomal enzymes were measured during the induction of tyrosine transaminase in rat liver by cortisone acetate. Tyrosine transaminase showed a maximum specific activity 2 h after the injection of the steroid hormone whereas lysosomal enzyme levels reached a maximum specific activity at 4 h. The maximum increase in specific activity for 15 injected animals compared to 15 controls was 100% for tyrosine transaminase; 40% for cathepsin A, cathepsin D, and β-N-acetylglucosaminidase; and 10% for acid phosphatase. Increased specific activities from livers of cortisone-acetate-treated rats were observed when lysosomal enzymes were released both by detergent treatment and by freezing and thawing.The increased specific activities were found in the readily solubilized lysosomal enzyme fractions and not in those lysosomal enzyme fractions which remain associated with particulate matter after lysosomal disruption. Similar increased specific activities for acid phosphatase and β-N-acetylglucosaminidase were observed in cultures of Morris hepatoma cells from rat liver when incubated with cortisone acetate in vitro. Thus the response appears to be typical of single cell types.

scholarly journals Gut Digestive Function and Microbiome after Correction of Experimental Dysbiosis in Rats by Indigenous Bifidobacteria

2021 ◽  
Vol 9 (3) ◽  
pp. 522
Author(s):  
Lyudmila V. Gromova ◽  
Elena I. Ermolenko ◽  
Anastasiya L. Sepp ◽  
Yulia V. Dmitrieva ◽  
Anna S. Alekseeva ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Digestive Enzymes ◽  
Specific Activity ◽  
Control Group ◽  
Enteropathogenic Escherichia Coli ◽  
Beneficial Bacteria ◽  
Opportunistic Bacteria ◽  
Dyspeptic Symptoms ◽  
Specific Activities ◽  
Impaired Motor Function

In recent years, great interest has arisen in the use of autoprobiotics (indigenous bacteria isolated from the organism and introduced into the same organism after growing). This study aimed to evaluate the effects of indigenous bifidobacteria on intestinal microbiota and digestive enzymes in a rat model of antibiotic-associated dysbiosis. Our results showed that indigenous bifidobacteria (the Bf group) accelerate the disappearance of dyspeptic symptoms in rats and prevent an increase in chyme mass in the upper intestine compared to the group without autoprobiotics (the C1 group), but significantly increase the mass of chyme in the colon compared to the C1 group and the control group (healthy animals). In the Bf group in the gut microbiota, the content of opportunistic bacteria (Proteus spp., enteropathogenic Escherichia coli) decreased, and the content of some beneficial bacteria (Bifidobacterium spp., Dorea spp., Blautia spp., the genus Ruminococcus, Prevotella, Oscillospira) changed compared to the control group. Unlike the C1 group, in the Bf group there was no decrease in the specific activities of maltase and alkaline phosphatase in the mucosa of the upper intestine, but the specific activity of maltase was decreased in the colon chyme compared to the control and C1 groups. In the Bf group, the specific activity of aminopeptidase N was reduced in the duodenum mucosa and the colon chyme compared to the control group. We concluded that indigenous bifidobacteria can protect the microbiota and intestinal digestive enzymes in the intestine from disorders caused by dysbiosis; however, there may be impaired motor function of the colon.

scholarly journals Transformation of the glucocorticoid receptor in rat liver cytosol by lysosomal enzymes.

1979 ◽  
Vol 254 (5) ◽  
pp. 1537-1539 ◽  
Author(s):  
J. Carlstedt-Duke ◽  
O. Wrange ◽  
E. Dahlberg ◽  
J.A. Gustafsson ◽  
B. Högberg
Keyword(s):  
Glucocorticoid Receptor ◽  
Rat Liver ◽  
Lysosomal Enzymes ◽  
Liver Cytosol ◽  
Rat Liver Cytosol

scholarly journals Biosynthesis of apolipoprotein C-III in rat liver and small intestinal mucosa.

1984 ◽  
Vol 259 (4) ◽  
pp. 2452-2456 ◽  
Author(s):  
M C Blaufuss ◽  
J I Gordon ◽  
G Schonfeld ◽  
A W Strauss ◽  
D H Alpers
Keyword(s):  
Rat Liver ◽  
Intestinal Mucosa ◽  
Small Intestinal Mucosa ◽  
Apolipoprotein C ◽  
Small Intestinal

Metabolism of acridine by rat-liver enzymes

1984 ◽  
Vol 140 (1) ◽  
pp. 7-11 ◽  
Author(s):  
Kenneth D. McMurtrey ◽  
Thomas J. Knight
Keyword(s):  
Rat Liver ◽  
Liver Enzymes

Pharmacologic perturbation of rat liver lysosomes: Effects on release of lysosomal enzymes and of lipids into bile

1988 ◽  
Vol 95 (4) ◽  
pp. 1088-1098 ◽  
Author(s):  
Richard B. Sewell ◽  
Susan A. Grinpukel ◽  
Alan R. Zinsmeister ◽  
Nicholas F. LaRusso
Keyword(s):  
Rat Liver ◽  
Lysosomal Enzymes ◽  
Liver Lysosomes ◽  
Rat Liver Lysosomes

Digestion and Digestive Enzymes in the Herring (Clupea harengus L.)

1935 ◽  
Vol 1 (3) ◽  
pp. 145-157 ◽  
Author(s):  
Helen I. Battle
Keyword(s):  
Intestinal Mucosa ◽  
Digestive Enzymes ◽  
Clupea Harengus ◽  
Acidic Condition ◽  
Pyloric Caeca ◽  
Temperature Range ◽  
Gastric Contents

Crustacean food is partially broken down and digested in the caecum of the stomach of the herring. It becomes more finely divided in the pyloric sac and consists of an oily chyme, intermingled with chitin, mucus and bacterial clumps in the pyloric caeca and intestine. The acidic condition of the gastric contents is probably instrumental in the reddening of chitinous food in the tract. Pepsin from the stomach and trypsin from the pyloric caeca increase in digestive power over a temperature range from 2.4 to 37.5 °C. The stomach secretes a protease (pepsin), a weak amylase, and possibly a weak lipase. The pyloric caeca secrete a strong protease (trypsin), a strong amylase, and a lipase rendered active by bile. The intestinal mucosa exhibits lipolytic and amylolytic ferments, while the bile has some amylolytic properties.

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