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- Hernell, Olle, et al.
(författare)
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Does the bile salt stimulated lipase of human milk have a role in the use of the milk long-chain polyunsaturated fatty acids?
- 1993
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Ingår i: Journal of Pediatric Gastroenterology and Nutrition - Jpgn. - 1536-4801 .- 0277-2116. ; 16:4, s. 426-431
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Tidskriftsartikel (refereegranskat)abstract
- Long-chain polyunsaturated (LCP) fatty acids derived from linoleic (18:2 n-6) and alpha-linolenic (18:3 n-3) acids are considered essential nutrients in preterm infants. The efficiency by which such fatty acids are released as absorbable products from triacylglycerol was explored in vitro using rat chylomicron triacylglycerol as substrate. When incubated with purified human pancreatic colipase-dependent lipase and colipase, arachidonic acid (20:4 n-6) was released less efficiently than linoleic acid from such triacylglycerol. This difference was not seen when purified human milk bile salt-stimulated lipase (BSSL) was incubated with the triacylglycerol substrate, and it was almost abolished when colipase-dependent lipase (with colipase) and BSSL acted simultaneously, as they do in breast-fed infants. There was no difference in arachidonic acid and eicosapentaenoic acid (20:5 n-3) release rates with either colipase-dependent lipase or BSSL, albeit the release was more rapid with the milk enzyme than with colipase-dependent lipase. Again, the most efficient release as absorbable free fatty acids was achieved when the two lipases operated together. The relative resistance to hydrolysis of arachidonic acid and eicosapentaenoic acid by colipase-dependent lipase was best explained by the localization of the first double bond to the delta-5 position of the respective fatty acid. The results obtained suggest that BSSL is of importance for the efficient use of human milk LCP fatty acids.
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| 6. |
- Bergström, Erik, et al.
(författare)
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Dietary changes in Swedish adolescents.
- 1993
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Ingår i: Acta Paediatrica. - 0803-5253 .- 1651-2227. ; 82:5, s. 472-80
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Tidskriftsartikel (refereegranskat)abstract
- A school-based dietary survey, using seven-day records, was performed in two cohorts of Swedish adolescents; 14- and 17-year-olds. The study comprised 366 boys and 365 girls. When compared to previous studies in Sweden, a striking finding was a decrease in dietary fat intake and an increase in carbohydrate intake. However, the relative intake of saturated fat had not changed (15% of total energy). The dietary change was mainly due to an increased consumption of cereal products. There were no major differences in dietary habits or nutrient density of the food between the two age groups, or between boys and girls. The mean intakes of protein, fat and carbohydrate, expressed as a percentage of the total energy intake, were 15, 33 and 52%, respectively. The mean intakes of vitamins and minerals were low only for selenium. The boys had a high iron intake (1.5 and 1.7 times the recommended intake for 14- and 17-year-olds, respectively) while the mean iron intake for girls was 0.9 times the recommended dietary allowances in both age groups. The intake of dietary salt was higher in boys than in girls (7.7 g and 9.0 g per day in 14- and 17-year-old boys, respectively, and 5.8 g per day in both 14- and 17-year-old girls). In a long-term health perspective, this positive change in nutrient intake in adolescents may contribute to a reduction in the incidence of diet-related diseases in Sweden.(ABSTRACT TRUNCATED AT 250 WORDS)
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| 7. |
- Bergström, S, et al.
(författare)
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Cloning and sequencing of human kappa-casein cDNA.
- 1992
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Ingår i: DNA Sequence. - 1042-5179 .- 1029-2365. ; 3:4, s. 245-6
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Tidskriftsartikel (refereegranskat)abstract
- A cDNA encoding kappa-casein of human milk was cloned and sequenced. The kappa-casein cDNA was isolated from a lambda gt11 library generated from mRNA prepared from a mammary gland biopsy obtained from a lactating woman. The library was screened with polyclonal rabbit antibodies raised against purified native kappa-casein. The obtained nucleotide sequence contained an ORF sufficient to encode the entire amino acid sequence of a kappa-casein precursor protein consisting of 182 amino acids. This includes a tentative signal peptide of 20 amino acids and a processed protein of 162 amino acids.
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| 8. |
- Bernbäck, S, et al.
(författare)
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The complete digestion of human milk triacylglycerol in vitro requires gastric lipase, pancreatic colipase-dependent lipase, and bile salt-stimulated lipase.
- 1990
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Ingår i: Journal of Clinical Investigation. - 0021-9738 .- 1558-8238. ; 85:4, s. 1221-6
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Tidskriftsartikel (refereegranskat)abstract
- Gastric lipase, pancreatic colipase-dependent lipase, and bile salt-stimulated lipase all have potential roles in digestion of human milk triacylglycerol. To reveal the function of each lipase, an in vitro study was carried out with purified lipases and cofactors, and with human milk as substrate. Conditions were chosen to resemble those of the physiologic environment in the gastrointestinal tract of breast-fed infants. Gastric lipase was unique in its ability to initiate hydrolysis of milk triacylglycerol. Activated bile salt-stimulated lipase could not on its own hydrolyze native milk fat globule triacylglycerol, whereas a limited hydrolysis by gastric lipase triggered hydrolysis by bile salt-stimulated lipase. Gastric lipase and colipase-dependent lipase, in combination, hydrolyzed about two thirds of total ester bonds, with monoacylglycerol and fatty acids being the end products. Addition of bile salt-stimulated lipase resulted in hydrolysis also of monoacylglycerol. When acting together with colipase-dependent lipase, bile salt-stimulated lipase contributed also to digestion of tri- and diacylglycerol. We conclude that digestion of human milk triacylglycerol depends on three lipases with unique, only partly overlapping, functions. Their concerted action results in complete digestion with free glycerol and fatty acids as final products.
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| 9. |
- Blind, Per-Jonas, et al.
(författare)
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Carboxylic ester hydrolase. A sensitive serum marker and indicator of severity of acute pancreatitis.
- 1991
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Ingår i: International journal of Pancreatology. - 0169-4197. ; 8:1, s. 65-73
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Tidskriftsartikel (refereegranskat)abstract
- When using clinical criteria, both falsely positive and falsely negative diagnoses of acute pancreatitis (AP) are often made. Based on a clinical study, elevated serum levels of the pancreatic lipolytic enzyme carboxylic ester hydrolase (CEH) was recently suggested to be a highly specific marker of acute pancreatitis. To determine the sensitivity of the test for AP, a study on patients with the diagnosis set objectively was necessary. In the present study, AP was diagnosed by contrast-enhanced computed tomography in 64 patients, and histopathological examination of tissue removed at laparotomy in 18 of them. By these criteria, 42 patients suffered from acute interstitial pancreatitis (AIP), and 22 patients from necrotizing pancreatitis (NP). Based on the CEH concentrations in the first serum sample obtained in each patient, the sensitivity of CEH for pancreatitis was 98%. From the second day after admission, CEH levels in patients with NP were significantly higher than in patients with AIP. Furthermore, in patients with NP, CEH values remained at a raised level for the following 10 d, whereas a significant decrease of CEH values was noted in patients with AIP. In contrast, total serum amylase activities were higher in patients suffering of AIP than in patients suffering of NP during the observation period. We conclude, that the sensitivity of the CEH test is very high for AP. CEH concentrations remaining at a high level are suggestive of NP, whereas diminishing CEH levels are suggestive of AIP.
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| 10. |
- Bläckberg, Lars, et al.
(författare)
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Bile salt-stimulated lipase in human milk. Evidence that bile salt induces lipid binding and activation via binding to different sites.
- 1993
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Ingår i: FEBS Letters. - : Wiley. - 0014-5793 .- 1873-3468. ; 323:3, s. 207-210
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Tidskriftsartikel (refereegranskat)abstract
- Human milk bile salt-stimulated lipase ensures efficient triacylglycerol utilization in breast-fed newborns. For activity against long-chain triacylglycerol, primary bile salts are a prerequisite. Bile salts also protect the enzyme from inactivation by intestinal proteases. We have studied the effect of different bile salts on activation, protease protection, lipid binding, and enzyme inactivation, caused by an arginine modifying agent. Based on the results we propose a model involving two bile salt binding sites; one activation-site specific for primary bile salt, and another, less specific, lipid binding promoting site at which also secondary bile salt binds. Binding to this latter site induces binding of enzyme to emulsified substrates but binding promoting site at which also secondary bile salt binds. Binding to this latter site induces binding of enzyme to emulsified substrates but without subsequent lipolysis.
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