Digestive Studies in Children

Borgström, Bengt

doi:10.1001/archpedi.1961.04020050044009

Cited by 23 publications

(3 citation statements)

References 16 publications

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“…This is in agreement with our previous in vitro studies (13) and also with in vivo studies in weanling rats (19). The slow digestion of bovine serum albumin is in agreement with the early findings by Borgström et al, who demonstrated that 5‐15% of human serum albumin was absorbed in the upper jejunum in preterm infants (8) and 30‐40% in 3‐ to 5‐month‐old term infants (22).…”

Section: Discussionsupporting

confidence: 90%

Digestion of Proteins in Human Milk, Human Milk Fortifier, and Preterm Formula in Infant Rhesus Monkeys

Lindberg,

Engberg,

Jakobsson

et al. 1997

J. pediatr. gastroenterol. nutr.

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Background:There is limited information in the literature on the capacity of the preterm infant to digest human and bovine milk proteins. We therefore studied in vivo the luminal phase of the hydrolysis of proteins in human milk, human milk fortifier, and preterm formula in preterm rhesus monkeys and in infant rhesus monkeys at 6 weeks and 7 months of age.Methods:Protein hydrolysis was followed by polyacrylamide gradient gel electrophoresis and electroimmunoassay. The serum level of absorbed unhydrolyzed human α‐lactalbumin was measured by a radioimmunoassay method. Trypsin and elastase activities in duodenal contents were measured before and after the meal.Results:In 6‐week‐old monkeys, the enzyme activities decreased by 50% postprandially, whereas they increased in 7‐month‐old monkeys. In preterm and in 6‐week‐old monkeys, hydrolysis of human and bovine whey proteins was slow, and in 6‐week‐old monkeys, 30‐50% of the proteins could still be detected immunochemically in duodenal contents after 60 min. At these ages, serum levels of absorbed α‐lactalbumin were high. At 7 months of age, no or small (lactoferrin and bovine serum albumin) amounts of the proteins could be detected in duodenal contents after 15 min. At this age α‐lactalbumin was not measurable in serum.Conclusion:The low capacity to digest whey proteins in suckling monkeys may depend upon an immaturity of the exocrine pancreas to respond to secretogogues.

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Section: Discussionsupporting

confidence: 90%

Digestion of Proteins in Human Milk, Human Milk Fortifier, and Preterm Formula in Infant Rhesus Monkeys

Lindberg,

Engberg,

Jakobsson

et al. 1997

J. pediatr. gastroenterol. nutr.

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“…Schedl and Clifton (1961) studied the kinetics of glucose absorption in two patients with idiopathic steatorrhoea, and from their report, which was only in abstract form, it would appear that they also found that it followed saturation kinetics. Absent or defective water absorption in the jejunum of patients with idiopathic steatorrhoea (Fordtran et al, 1961) and also in children with coeliac disease (Borgstrom, Lindquist, and Lundh, 1961) has been reported previously. To compensate for this, there is a greater net water absorption in the ileum of these patients than in normal subjects (Schedl and Clifton, 1963).…”

Section: Discussionmentioning

confidence: 58%

Glucose and fructose absorption in idiopathic steatorrhoea.

Holdsworth¹,

Dawson²

1965

Gut

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“…To the best of our knowledge, this is the first study investigating the luminal phase of the breakdown of the cow's milk proteins a-lactalbumin and {3-lactoglobulin in the upper part of the gastrointestinal tract during infancy. It has been shown in the classic studies by Borgstrom et al (17) that 30-40% of the protein is digested and absorbed in the upper part of the jejunum in infants.…”

Section: Discussionmentioning

confidence: 99%

In Vitro Digestion of Cow's Milk Proteins by Duodenal Juice from Infants with Various Gastrointestinal Disorders

Jakobsson,

Lindberg,

Benediktsson

1982

J. pediatr. gastroenterol. nutr.

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The hydrolysis of bovine α‐lactalbumin, β‐lactoglobulin, and casein by duodenal juice from 20 infants (18 with normal exocrine pancreatic function, 2 with pancreatic insufficiency), aged 3–19 months was studied in vitro with the aid of electroimmunoassay and sodium dodecyl sulfate–poly‐acrylamide gel electrophoresis. The results from the two methods were almost identical. Duodenal juice from infants with cow's milk protein intolerance (7), celiac disease (5), and unclassified gastrointestinal disorder (6) had the same capacity to hydrolyze the milk proteins. No hydrolysis occurred in the two patients with pancreatic insufficiency. The hydrolyzing capacity was not correlated with age in the actual age group. The hydrolysis of the milk proteins occurred at a considerably slower rate when the proteins were crude, as in cow's milk, adapted, or unadapted formula, than when they were in a purified form. About 1 mg of purified α‐lactalbumin or β‐lactoglobulin, and about 30 mg of purified casein could be hydrolyzed per milliliter duodenal juice per minute. Corresponding figures for the hydrolysis of the various proteins in cow's milk were 0.03, 0.12, and 16.1 mg/ml duodenal juice/min. Preincubation (60 min) with gastric aspirate after adjusting pH to 4–5 did not change the results. In conclusion, the duodenal juice from infants with normal exocrine pancreatic function has a great ability to hydrolyze casein. Corresponding hydrolytic capacity for α‐lactalbumin or β‐lactoglobulin is considerably lower.

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Digestive Studies in Children

Cited by 23 publications

References 16 publications

Digestion of Proteins in Human Milk, Human Milk Fortifier, and Preterm Formula in Infant Rhesus Monkeys

Digestion of Proteins in Human Milk, Human Milk Fortifier, and Preterm Formula in Infant Rhesus Monkeys

Glucose and fructose absorption in idiopathic steatorrhoea.

In Vitro Digestion of Cow's Milk Proteins by Duodenal Juice from Infants with Various Gastrointestinal Disorders

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