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Biomedical subjects

T Lindberg

Publications and source records attributed to T Lindberg.

At least 91 records · Page 5Linked to original sources

Small intestinal dipeptidases and disaccharidases in experimental uremia in rats.

Rats were made severely uremic with partial nephrectomy (24-hour creatinine clearance 10% of normal). Jejunal dipeptidase activities (substrates: glycyl-L-leucine, L-alanyl-L-proline, and L-methionyl-L-methionine), disaccharidase activities (maltase, sucrase, trehalase, and lactase) and morphology were studied. A highly significant increase in glycyl-L-leucine and L-methionyl-L-methionine dipeptidases was found in uremic rats compared with controls. Proline dipeptidase activities were unaltered. Disaccharidase activities showed a slight increase in sucrase in uremic rats; otherwise no change was found.

Animals↗

Lung function in cystic fibrosis: acute effect of salbutamol.

Pulmonary function tests including spirometry, N2 washout and volume of trapped gas (VTG) were obtained in 12 children with cystic fibrosis (CF), 6-18 years of age, before and after inhalation of 0.2 mg salbutamol. 11 children had pathologically increased VTG while the lung clearance index (LCI) was abnormal in 9, V'max 25/TLC (maximal flow at 25% of vital capacity/total lung capacity) in 8, residual volume in 6, but FEV1 in only 2 children. VTG/TLC% increased with age while V'max 25/TLC and FEV1 did not change. Neither was clinical score related to age in our subjects. No improvement in lung function occurred after salbutamol inhalation. VTG proved most sensitive for showing abnormality in children with CF.

Adolescent↗

Immunichemical determination of cathodal elastase in human duodenal juice.

In human duodenal juice enzymes hydrolysing the elastase substrate succinyl-trialanine-p-nitroanilide have both an anodal and cathodal mobility in agarose gel electrophoresis. The cathodal enzyme, also having an elastinolytic activity, was purified. An application of electroimmunoassay for separate determination of this cathodal elastase is presented. Parallel estimations of esterolytic, elastinolytic and immunochemical activities in duodenal juice from a group of children revealed discrepancies suggesting both variations in the distribution of the two forms of "elastases", and presence of inactive forms.

Adult↗

Influence of food on the absorption of phenytoin in man.

The influence of food intake on the absorption of phenytoin was examined in eight healthy volunteers, by study of single-dose kinetics following ingestion of phenytoin 300 mg either with a standardized breakfast or on an empty stomach. Blood samples were collected at regular intervals from 0 to 48 h, and serum concentrations of unmetabolized phenytoin were determined by gas chromatography. Serum concentrations of the major metabolite of phenytoin, 4-hydroxyphenytoin, were measured by mass fragmentography. Concurrent intake of food and phenytoin appeared to accelerate absorption of the drug from the formulation used, and the peak concentrations were significantly higher (mean increase 40%) in the postprandial than in the preprandial state. As reflected by the AUC (area under the curve), the amount of drug absorbed was increased during postprandial conditions, although the difference only reached borderline significance. It is suggested that phenytoin should always be taken in a defined relation to meals.

Adult↗

Immunochemical determination of two trypsins in human duodenal juice.

An application of electroimmunoassay to the separate determination of anionic and cationic trypsin in human duodenal juice is presented. The proportions of anionic to cationic immunoactive trypsin in duodenal juice from a group of children averaged 20 : 80. The ratio of immunoactive to esterolytically (BAPNA) active trypsin averaged 1.6 : 1, indicating the presence of inactive forms of trypsin in duodenal juice.

Child↗

In vivo absorption of phenytoin from rat small intestine and its inhibition by phlorizin.

In vivo absorption of phenytoin from the small intestine was studied by an in vivo closed segment technique. Phenytoin in concentrations of 1000, 2000, and 4000 mumol/l was administered in dissolved form. Polythylene glycol 4000 was used as a non-absorbable marker. The concentrations of phenytoin in the intestinal lumen, in the mucosa, and in cardiac blood were measured both by spectrophotometry and by gas chromatography. Phenytoin was absorbed very rapidly, and the proportion absorbed increased with increasing dose. Thus, during the first 10 min. about 85 per cent of the largest dose but only 25 per cent of the smallest dose had been absorbed. The phenytoin concentration in mucosa and serum increased in an analogous way; maximum values were observed within the first ten minutes. The concentrations in mucosa and serum were dose dependent during the first ten minutes. 0.01 mmol/l and 1 mmol/l phlorizin significantly reduced the transfer of phenytoin (4000 and 2000 mumol/l) from the gut lumen to the mucosa. No inhibition was observed when the initial phenytoin dose was 1000 mumol/l. The results suggest that an active transport mechanism, sensitive to phlorizin, is involved in the intestinal absorption of phenytoin in the rat.

Animals↗

Incidence of coeliac disease and transient gluten intolerance in children in a Swedish urban community.

The incidence of coeliac disease in children in the city of Malmö, South Sweden, was 1 : 982 during 1966 to 1975. The diagnostic criteria were: flat intestinal mucosa on gluten-containing diet, free of symptoms, and improvement in mucosal morphology on gluten-free diet, and morphological and/or evident clinical relapse (three times) on gluten challenge. 6 (12%) of 49 children with initially a flat mucosa still had a normal mucosa on a gluten-containing diet for two years or longer, having so-called transient gluten intolerance.

Celiac Disease↗

A prospective study of cow's milk protein intolerance in Swedish infants.

1 079 of 1 548 newborn infants were followed during their first year. 328 were prospectively contacted once a month. 751 were followed up at child welfare clinics. Altogether 20 were diagnosed as being cow's milk protein intolerant (1.9%). Symptoms from the gastrointestinal tract and the skin predominated. Only 2 had respiratory symptoms. Ten had their symptoms within one week after the introduction of cow's milk, 3 of them at their first cow's milk-containing meal. A further 4 already had symptoms when fed only human milk. The others (6 infants) showed symptoms after more than one week on a cow's milk containing diet. Before 2 years of age, 13 had recovered. Twelve of the cow's milk protein intolerant infants also showed adverse reactions to other foods, soy-protein intolerance being the most common (7 infants). A family history of allergy was found in 35% (116) of the 328 infants and in 70% (14) of those with cow's milk protein intolerance.

Age Factors↗

A child's experience of imminent death.

We relate here the experiences and thoughts of a 7-year-old girl about her situation during the last three months of life as she lay dying of Ewing's sarcoma. Our experience with this girl--and that of other children in the same situation--indicates that they have a realistic and even confident view of death. Their anxiety is centred on the disease and how it affects their appearance and their activity. We most often underestimate children's capacity for understanding their own situation. We ought to be sensitive to appeals for contract.

Attitude to Death↗

Do pre- and postchallenge small intestinal biopsies help to diagnose cow's milk protein intolerance?

Twelve infants suspected of cow's milk protein intolerance were challenged with cow's milk after at least one month of cow's milk-free diet. The challenge was clinically positive in seven. Small intestinal biopsies were taken with a multipurpose capsule both pre- and postchallenge (at 24 h) in eight, prechallenge in three, and postchallenge in one. Two or three biopsy specimens were taken at the same time in 15 of the 20 biopsy occasions. The morphology of the mucosa could vary from normal to slight damage at the same biopsy occasion. No difference was found in morphology judged by light microscopy between pre- and postchallenged biopsies. Light microscopy of small intestinal biopsies taken before and at 24 h after milk challenge seems of doubtful value as a routine diagnostic means in cow's milk protein intolerance.

Animals↗

A boy with severe infantile gastrogen lactose intolerance and acquired lactase deficiency.

A 10-year-old boy with severe familial lactose intolerance in infancy (vomiting, failure to thrive, lactosuria (5.25 g/l), sucrosuria (12 g/l), and aminoaciduria. Intestinal disaccharidases (including lactase and sucrase) normal at age 6 and 20 weeks. Oral lactose tolerance test at this age resulted in lactosuria (4.6 g/l); sucrose tolerance test, in sucrosuria (18.5 g/l). In contrast, intraduodenal lactose tolerance test gave only low lactose excretion in urine (0.28 g/l). He improved rapidly and had no lactosuria on intraduodenal feeding with citric acid milk. The lactosuria diminished as age increased, but was still higher at age 6 years than that of controls. He tolerated normal disaccharide containing food after 1.5 years of age. At 5.5 to 6 years, he had symptoms of lactose malabsorption, and an isolated lactase deficiency was proved. At 10 years, he still tolerates only limited amounts of milk. The defect in severe familial infantile lactose intolerance seems to be localized in the gastric mucosa. Acquired lactase deficiency can appear later in childhood in this syndrome.

Amino Acids↗

Protease inhibitors in human milk.

Protease inhibitors (inhibiting trypsin, chymotrypsin, and elastase) were demonstrated in human milk from birth to 4 months after delivery. No pepsin inhibitor was found. The protease inhibitors were localized in the alpha 1-region--inhibiting trypsin, chymotrypsin, and elastase--and in a more cathodal region--inhibiting chymotrypsin--in agarose gel electrophoresis of human milk. alpha 1-antitrypsin and antichymotrypsin were demonstrated by crossed immunoelectrophoresis. Electroimmunoassay showed the concentration of alpha 1-antitrypsin in 1st day milk to be 10.9% and the concentration of antichymotrypsin was 116% of that of adult serum. The concentrations decreased during the 1st wk; from 1 wk to 4 months they were 1.6% for alpha 1-antitrypsin and 3.8% for antichymotrypsin of those of adult serum. One ml of human milk from the first 3 days inhibits, by enzymatic methods, 0-150 microgram (mean value, 70 microgram) trypsin. Milk from 1 week after delivery and later inhibits 0-65 microgram (mean value, 38 microgram) trypsin per ml.

Animals↗

Agarose gel electrophoresis of duodenal juice in normal condition and in children with malabsorption.

Agarose gel electrophoresis (at pH 8.6) was used for qualitative determination of pancreatic enzymes in duodenal juice. The various enzymes were identified by staining techniques with specific chromogenic substrates, by quantitative determination of enzymes in eluates of gel slices, and by immunoelectrophoresis. The various protein bands corresponded to the following enzymes (from the anode to the cathode): chymotrypsin, trypsin, carboxypeptidase A, chymotrypsin, amylase (around the slit), lipase, elastase, and trypsin. The method was applied to a study of exocrine pancreatic function in 10 adults and 83 children suspected of having malabsorption. The duodenal juice, also analyzed for trypsin and amylase content, was collected in fasting condition and after a test meal of water. In patients with normal pancreatic function, all the enzyme bands were present and easy to recognize. In 87 patients carboxypeptidase A was present as two bands in 68 (80%), anodal trypsin as two bands in 39 (45%), and cathodal trypsin as two bands in 85 (97%). Electrophoresis of duodenal juice gave as much information from the fasting sample as after the test meal. Six children with pancreatic insufficiency (cystic fibrosis and Shwachmar's syndrome) had no or only faintly stained enzyme bands and a strongly stained albumin-containing band most anodally. The method is simple, rapid, and useful in routine work. The combination of this qualitative test with a quantitative one (e.g. trypsin determination) provides good information about exocrine pancreatic function.

Adolescent↗

Cow's milk as a cause of infantile colic in breast-fed infants.

18 mothers of 19 breast-fed infants with infantile colic were put on a diet free of cow's-milk protein. The colic disappeared promptly from 13; in 12, it reappeared on at least two further indirect challenges (in the form of a diet containing cow's milk to the mother). Most infants became symptom-free at age 2 to 4 months; at 4 months, only 4 reacted with colic when the mother took cow's milk. 5 infants were directly challenged with cow's milk; 4 reacted promptly with colic. Other signs of intolerance to cow's-milk protein developed in 3 infants during weaning. The treatment of infantile colic in breast-fed infants by a diet free of cow's milk for the mother appears worthwhile.

Adult↗