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Träfflista för sökning "swepub ;lar1:(umu);pers:(Hernell Olle);srt2:(1985-1989)"

Sökning: swepub > Umeå universitet > Hernell Olle > (1985-1989)

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  • Bernbäck, S, et al. (författare)
  • Bovine pregastric lipase : a model for the human enzyme with respect to properties relevant to its site of action.
  • 1987
  • Ingår i: Biochimica et Biophysica Acta. - 0006-3002. ; 922:2, s. 206-13
  • Tidskriftsartikel (refereegranskat)abstract
    • Preduodenal lipolysis is considered to promote efficient lipid digestion in the neonatal period. The lipase(s) responsible may be of pregastric or gastric origin depending upon the species. We have previously reported on purification and molecular characterization of a pregastric lipase from calf. Antibodies to this bovine enzyme crossreact with a protein of similar size in human gastric contents and also inhibit its lipolytic activity. Since the bovine and human enzymes also have similar kinetic properties, the view is favoured that the bovine enzyme can be used as a model for physiological studies relevant to human neonates. In contrast to the lipases operating in the small intestine pregastric lipase has the unique property of initiating the hydrolysis of human milk fat globule triacylglycerol. In order to do this no cofactor is required. Pregastric lipase was stable at low pH and had an acid-pH optimum. Furthermore, it was extremely resistant to pepsin. In contrast, pancreatic proteinases, i.e. trypsin and chymotrypsin, inactivated the enzyme. The rate of inactivation was increased in the presence of bile salts which by themselves could inhibit enzyme activity. Thus, pregastric lipase is ideally suited for activity in the stomach but will not, under healthy conditions, contribute to lipid digestion in the duodenum.
  • Bernbäck, S, et al. (författare)
  • Fatty acids generated by gastric lipase promote human milk triacylglycerol digestion by pancreatic colipase-dependent lipase.
  • 1989
  • Ingår i: Biochimica et Biophysica Acta. - 0006-3002. ; 1001:3, s. 286-93
  • Tidskriftsartikel (refereegranskat)abstract
    • The concerted action of purified bovine gastric lipase and human pancreatic colipase-dependent lipase and colipase, or crude human pancreatic juice, in the digestion of human milk triacylglycerols was explored in vitro. Gastric lipase hydrolyzed milk triacylglycerol with an initially high rate but became severely inhibited already at low concentration of released fatty acid. In contrast, colipase-dependent lipase could not, by itself, hydrolyze milk triacylglycerol. However, a short preincubation of milk with gastric lipase, resulting in a limited lipolysis, made the milk fat triacylglycerol available for an immediate and rapid hydrolysis by pancreatic juice, and also for purified colipase-dependent lipase, provided colipase and bile salts were present. The same effect was obtained when incubation with gastric lipase was replaced by addition of long-chain fatty acid. Long-chain fatty acid increased the binding of colipase-dependent lipase to the milk fat globule. Binding was efficient only in the presence of both fatty acid and colipase. We conclude that a limited gastric lipolysis of human milk triacylglycerol, resulting in a release of a low concentration of long-chain fatty acids, is of major importance for the subsequent hydrolysis by colipase-dependent lipase in the duodenum.
  • Blind, Per Jonas, et al. (författare)
  • Carboxylic ester hydrolase : a serum marker of acute pancreatitis
  • 1987
  • Ingår i: Pancreas. - 0885-3177. ; 2:5, s. 597-603
  • Tidskriftsartikel (refereegranskat)abstract
    • By use of an enzyme-linked immunosorbent assay we established serum reference values of carboxylic ester hydrolase, a pancreatic secretory lipolytic enzyme, and explored to see if a raised serum level is indicative of acute pancreatitis. Postoperative elevation of carboxylic ester hydrolase was observed in seven out of ten patients who underwent pancreatic surgery. Serum levels of carboxylic ester hydrolase and amylase were determined in 129 patients admitted due to abdominal emergency conditions. Amylase was elevated in 27 patients, and in 20 of these raised carboxylic ester hydrolase levels affirmed the diagnosis acute pancreatitis. In five out of the seven patients with elevated amylase alone no etiologic factor of acute pancreatitis was found. Another 11 patients had raised carboxylic ester hydrolase levels without concomitant elevation of amylase. In all these patients, a likely cause of pancreatic inflammation was identifiable. Hence, a raised carboxylic ester hydrolase level, even in presence of normal amylase, could be indicative of acute pancreatic inflammation.
  • Bläckberg, L, et al. (författare)
  • Bile-salt-stimulated lipase in human milk : evidence for its synthesis in the lactating mammary gland.
  • 1987
  • Ingår i: FEBS Letters. - 0014-5793. ; 217:1, s. 37-41
  • Tidskriftsartikel (refereegranskat)abstract
    • Human milk contains many enzymes and other biologically active proteins. One of the enzymes, the bile salt-stimulated lipase, constitutes as much as 1% of the milk proteins. Its importance for efficient utilization of milk lipids by the breast-fed infant is now well established. However, whether the lipase protein is a product of protein synthesis within the mammary gland has up till now been an unanswered question. Using biopsy material from lactating human mammary gland we have now demonstrated that the enzyme is synthesized within the gland. This was done by immunoprecipitation of [35S]methionine-labelled protein from tissue pieces. By activity determination we could also determine the amount of enzyme stored in the gland. It was concluded that bile salt-stimulated lipase accounted for 1.3 micrograms/mg tissue protein. Finally, from this figure it could be calculated that about 10-15% of the total protein present in the tissue was milk protein.
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  • Resultat 1-5 av 5
Typ av publikation
tidskriftsartikel (5)
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refereegranskat (5)
Bläckberg, Lars, (4)
Bernbäck, S (3)
Blind, Per-Jonas, (1)
Ljungberg, Börje, (1)
Bläckberg, L (1)
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Angquist, K-A, (1)
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Engelska (5)


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