Search PubMed⌕ Search

Biomedical subjects

C Bode

Publications and source records attributed to C Bode.

At least 217 records · Page 12Linked to original sources
PubMed1982

Activities of cytoplasmic, mitochondrial and brush border enzymes in jejunal mucosa of chronic alcoholics.

The activity of certain enzymes of the energy producing metabolism of the cytoplasmic and mitochondrial compartment and of disaccharidases was determined in jejunal biopsies of 24 chronic alcoholics (CA) and 10 non-alcoholic control subjects (C). The activity of glucokinase, an enzyme of glycolysis, was markedly (44%, p less than 0.05) increased in the biopsies obtained from CA, while the activity of fructose bisphosphatase, an enzyme of gluconeogenesis, was significantly (p less than 0.05) depressed in CA when compared to C. The activity of other glycolytic enzymes was not affected in CA. The activity of L-alanine amino-transferase was lower in CA (p less than 0.05). A reduction was also seen for mean succinate dehydrogenase activity in CA (-30%), however, this difference was not statistically significant. The mean activity of lactase, maltase and sucrase was comparable in both groups.

Alanine Transaminase↗
PubMed1981

Influence of feeding fructose on fructose and glucose absorption in rat jejunum and ileum.

The influence of feeding isocaloric diets containing either 65% of fructose (F 65) on 65% of glucose (G 65) were studied on the uptake of both sugars in segments of rat proximal jejunum and distal ileum. The hexose absorption was compared to that obtained in animals receiving isocaloric amounts of a diet containing 30% of glucose (G 30). Feeding fructose (F 65) for 3 days resulted in a 2.5-fold increase of fructose uptake in the jejunum and a 40% increase in the ileum as compared to group G 30. When fructose (F 65) was administered instead of G 65 the uptake of fructose was enhanced by 75% in the jejunum and 35% in the ileum. Stimulation of glucose absorption in segments of the proximal and distal small intestine by diets F 65 and G 65 was nearly identical as compared to the values of group G 30. The stimulation of the uptake of fructose induced by fructose feeding parallels an adaptive increase in the activity of enzymes involved in fructose metabolism in the mucosa of the small intestine.

Animals↗
PubMed1981

The pattern of D-galactosamine-induced hepatocellular injury modified by simultaneous application of D (--)-fructose.

As shown by light and electron microscopy, and by biochemical investigation, D-galactosamine-induced hepatocellular injury in the rat can be prevented by giving fructose simultaneously. However, when injected 3 h after D-galactosamine, fructose has no protective effect. It is suggested that rapid fructose phosphorylation, with the consequent marked depression of the hepatocellular ATP pool, inhibits the more prolonged D-galactosamine phosphorylation and with it the injurious effects of D-galactosamine metabolism.

Animals↗
PubMed1981

Effect of fructose feeding on the activity of enzymes of glycolysis, gluconeogenesis, and the pentose phosphate shunt in the liver and jejunal mucosa of rats.

The influence of fructose feeding for 1 to 12 days on the activity of enzymes of glycolysis and gluconeogenesis was studied in the jejunal mucosa and the liver of rats. In the jejunal mucosa fructose feeding leads to an increase in the activity of 6-phosphofructokinase (p less than 0.05) and fructose-1.6-bisphosphate aldolase (p less than 0.05), while the activity of hexokinase and glucose-6-phosphate dehydrogenase remains unchanged. Fructose feeding increases the activity of fructose-bisphosphatase in the jejunal mucosa, however, the absolute values of this enzyme remain low (less than 10%) when compared to those in the liver. In the liver fructose feeding is followed by a marked increase of the activity of fructose-bisphosphatase and glucose-6-phosphate dehydrogenase. In contrast, the activity of glucose-6-phosphatase decreases significantly under a fructose enriched diet. The enzyme activity rose to a maximum within 3 days; in the following time of observation no major changes occurred. The results are in accordance with the assumption that fructose feeding leads in the jejunal mucosa mainly to adaptive alterations of the activity of those enzymes which are involved in the breaking-down of fructose, whereas in the liver the activity of those enzymes is increased, which take part in the new synthesis of glucose-6-phosphate or which direct glucose-6-phosphate into the pentose-phosphate.

Animals↗
PubMed1980

Adaptative changes of activity of enzymes involved in fructose metabolism in the liver and jejunal mucosa of rats following fructose feeding.

The adaptative response of a diet containing 60% fructose on the activity of those enzymes which are involved in the metabolism of fructose was measured in the liver and in the jejunal mucosa of rats over a period of 12 days. Control animals received isocaloric amounts of glucose or starch. Under fructose feeding there was a marked increase in the activity of fructose-1-phosphate aldolase (3-fold), ketohexokinase (2--3-fold), and triokinase (3-fold) in the jejunal mucosa. In the liver, however, a significant increase in enzyme activity could only be seen for triokinase (2--3-fold), whereas the activity of the other enzymes measured were only slightly or not at all altered. The activity of the three enzymes mentioned above were elevated to a maximum within 3 days after feeding the fructose diet. In the following time of observation no major further changes occurred. The results show that fructose feeding in comparison to a glucose or starch containing diet leads to a marked adaptative increase in the activity of those enzymes, which are involved in the breakdown of fructose, only in the jejunal mucosa.

Alcohol Oxidoreductases↗
PubMed1980

Damage of rat small intestine induced by ethanol. Effect of ethanol on fecal excretion of intestinal alkaline phosphatase.

Single administration of ethanol or alcoholic beverages (5g ethanol/kg body weight) induces a decrease of the 24h excretion of fecal intestinal alkaline phosphatase (I-AP) activity of 28% (P less than 0.05) in comparison to controls (0.9% saline). Administration of higher amounts of 20% (v/v) ethanol (8g/kg body weight on 3 consecutive days) yields a decrease of fecal I-AP excretion up to 82% (P less than 0.005) in comparison to controls (saturated glucose solution). The interpretation of these results as a toxic effect of ethanol to small intestinal mucosa was supported by measurement of enzymatic activity in the small intestinal mucosa and by morphometric data.

Alkaline Phosphatase↗
PubMed1979

Alcohol metabolism in man: effect of intravenous fructose infusion on blood ethanol elimination rate following stimulation by phenobarbital treatment or chronic alcohol consumption.

The effect of phenobarbital (PB) pretreatment and of chronic alcoholism on blood ethanol elimination rate (BEER) was investigated in man. In order to gain additional information concerning the mechanism of possible changes BEER was determined before and during intravenous infusion of fructose, a compound known to increase the NADH-oxidizing capacity of the liver and thereby stimulating alcohol oxidation rate. Following PB-treatment (300 mg/day for 5-6 days, n = 8) a marked increase in unstimulated (U-) BEER was obtained. But the fructose stimulated (FS-) BEER was not significantly changed by PB-treatment. In chronic alcoholics (n = 15) U-BEER values above the upper limit (chi + 2 S D) obtained in healthy controls, were observed only when the time of sobriety was less than one week (n = 6). Values of FS-BEER in chronic alcoholics with increased basal alcohol oxidation rates were in the same range as those of healthy controls. In 5 out of the 6 alcoholics in whom the values were elevated on admission, BEER decreased significantly after withdrawal of alcohol for 2-4 weeks. Since FS-BEER was nearly identical in all conditions tested, the distinct changes in U-BEER are probably independent of changes in the activity of enzymes involved in alcohol oxidation. It is assumed that alcohol metabolism in man is mainly controlled by the rate of NADH reoxidation in the liver.

Adult↗
PubMed1979

Primary hyperparathyroidism in a dog.

A 6-year-old male Standard Poodle had hypercalcemia, hypophosphatemia, and a urinary concentrating defect. A parathyroid adenoma involving the left caudal parathyroid gland was surgically removed. Transient hypocalcemia followed, which resolved without treatment. A renal biopsy did not demonstrate renal parenchymal mineral deposition. Urinary concentrating ability returned after surgery.

Adenoma↗
PubMed1978

[The question of use of glucose or fructose for parenteral feeding. Results of a comparative study].

Glucose and fluctose (400 g/24 h) were compared as sources of carbohydrate in parenteral nutrition in patients following major abdominal operations or following multiple injuries. Group A (n = 8) received glucose during the first 2 days and fructose for another 2 days thereafter. In group B (n = 8) the sequence of carbohydrate infusion was reversed (2 days' fructose follwed by 2 days' glucose). The additional infusion to amino acids and a fat emulsion remained constant (total calories: 2,700 kcal/24 h). The following results were obtained: 1. Mean blood glucose concentrations were elevated in both infusion periods. During infusion of glucose the values were about 10% higher than those obtained during fructose infusion. Insulin administration was not necessary any of the patients studied. 2. Urinary excretion of both monosaccharides was negligible. 3. Blood lactate concentrations were higher during the infusion of fructose when compared to the glucose infusion period. The concentration of ketone bodies in the blood was not significantly influenced by either regimen. No major changes in base-acid equilibrium were observed. 4. The serum concentration of uric acid and several other metabolites did not differ significantly during the two infusion periods. 5. Mean urinary urea excretion exhibited a 30% increase during fructose infusion when compared to the glucose infusion period (p less than 0.012). From the results of t;is study and earlier findings it is concluded that fructose in a dose up to 400 g/day has no proven advantages over glucose in postoperative parenteral nutrition.

Adolescent↗
PubMed1978

Effect of alcohol on microsomal cortisol 4en-5 alpha-reductase in the liver of rats fed on a standard or low protein diet.

Alcohol feeding (40% of total calories over a period of 9 days) increases microsomal cortisol-5 alpha-reductase activity in rat liver distinctly. It is assumed that this is an adaptive response to an increased release of cortisol caused by alcohol administration. Cortisol-5 alpha-reductase activity is decreased to one third of control values in rats fed an isocaloric, low protein diet. The response to alcohol feeding is susta ined in these animals. Phenobarbital treatment (80 mg/kg x day) stimulates 5 alpha-reduction of cortisol per g of microsomes almost twofold. The activity calculated per total liver increases 4-fold. Alcohol administration has no additional effect on cortisol-5alpha-reductase in phenobarbital-treated rats.

Animals↗
PubMed1978

A comparison between naturally occurring macroamylasaemia and macroamylasaemia induced by hydroxyethyl-starch.

Macroamylasaemia was produced in vitro by incubation of hydroxyethylstarch with serum, and in vivo by intravenous infusion of hydroxyethylstarch. Gel filtration on Sephadex G-100 revealed distinct differences in molecular size distribution between such hydroxyethylstarch-induced macroamylase and the usual form of naturally occurring macroamylase which was observed in a few patients from our hospital. Further studies demonstrated that the gel filtration elution pattern of amylase activity in serum containing hydroxyethylstarch-induced macroamylase is significantly altered with time in vitro and in vivo, probably because of an enzymatic degradation of the hydroxyethylstarch components of the macromolecular complexes. In a healthy volunteer the serum amylase activity was elevated to a maximum of 797 u/l and the renal clearance rate of amylase was diminished to a minimum of 0.3 ml/min after infusion of 500 ml of a 6% solution of hydroxyethylstarch, as compared to 300 u/l, and 0.95 ml/min, respectively, during the pre-infusion period.

Adult↗
PubMed1978

Fecal chymotrypsin: study on some characteristics of the enzyme.

A Lineweaver-Burk plot demonstrated that the apparent Michaelis constants are identical for chymotrypsin (CT) in duodenal juice and in feces of the same patient. CT in fecal homogenates exhibits exhibits a remarkable stability and is bound to particles to a considerable but variable extent. The pH optimum of CT in human feces is somewhat higher as compared to pure bovine pancreatic CT. All measurements of fecal CT activity should, therefore, be performed at pH 9.0. The distribution of CT among the fecal mass has been investigated. There were considerable differences between CT activities in random fecal specimens and in the corresponding stool collections. However, if the results were expressed in terms of 'normal' and 'abnormal', 113 out of 120 random fecal specimens gave the same results as the corresponding stool collections. It is concluded that the risk of 'false-normal' values cannot be effectively reduced by determination of CT outputs in stool collections (or by using continuous markers) instead of CT activities in random stool specimens.

Chymotrypsin↗
PubMed1977

A controlled trial of glucagon in acute experimental pancreatitis in rats.

Acute pancreatitis was induced in 245 rats by retrograde instillation of Na-taurocholate into the pancreatic duct. Mortality rate in animals treated 6-hourly with glucagon (1 mg/kg) after induction of pancreatitis was 50% as compared to 30% deaths in the controls treated with 0,9% NaCl (chi2-test: p less than 0,05). Mortality rate in animals treated 6-hourly with the same dose of glucagon before induction of pancreatitis was 36,5% as compared to 28% deaths in the corresponding controls (chi2-test: p greater than 0,05). Glucagon in lower doses (0,1-0,5 mg/kg every 6 hours) did not alter mortality rates as compared to animals treated with 0,9% NaCl. 2. A nonletal form of pancreatitis was induced in 26 rats by ligation of the pancreatic duct. Injection of glucagon (1 mg/kg) seemed to suppress amylase activities in blood for a short period of appr. 1 hour. However, 7 and 9 hours after induction of pancreatitis, amylase activities were significantly higher in animals treated one or two times with glucagon as compared to untreated controls. It is concluded that glucagon in the high dose of 1-4 mg/kg/24 hours does not only not influence the course of acute experimental pancreatitis in rats but can even deteriorate it.

Acute Disease↗