Proteolytic inactivation of lipase as a possible cause of the uneven results obtained with enzyme substitution in pancreatic insufficiency. | |
MedLine Citation:
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PMID: 6199274 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Inactivation of lipase in four commercially available pancreatin preparations in buffer solution, in duodenal juice stimulated by secretin-cholecystokinin or by Lundh test-meal, and in duodenal juice supplemented with a meat-meal homogenate, was examined during a four-hour incubation period. In the buffer solution and in the secretin-cholecystokinin-stimulated duodenal juice 64-89% of lipase activity was already lost within two hours. Trypsin activity was in inverse relation to that of lipase and soybean trypsin inhibitor. The Lundh test meal and the meat-meal homogenate significantly diminished inactivation of lipase. Substitution therapy of pancreatic insufficiency with crushed and soybean-trypsin-inhibitor supplemented preparations diminished steatorrhoea more effectively than the simple tablets. The demonstrated proteolytic inactivation of lipase indicates that pancreatic supplements have to be given in crushed or granulated form, well mixed with protein-containing meals, and that a physiological ratio of trypsin-lipase activity ought to be preserved in the preparations. |
Authors:
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A Pap; V Varró |
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Publication Detail:
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Type: Clinical Trial; Journal Article |
Journal Detail:
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Title: Hepato-gastroenterology Volume: 31 ISSN: 0172-6390 ISO Abbreviation: Hepatogastroenterology Publication Date: 1984 Feb |
Date Detail:
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Created Date: 1984-04-06 Completed Date: 1984-04-06 Revised Date: 2007-11-15 |
Medline Journal Info:
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Nlm Unique ID: 8007849 Medline TA: Hepatogastroenterology Country: GERMANY, WEST |
Other Details:
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Languages: eng Pagination: 47-50 Citation Subset: IM |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
MeSH Terms | |
Descriptor/Qualifier:
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Amylases
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analysis Celiac Disease / drug therapy, enzymology Chronic Disease Clinical Trials as Topic Exocrine Pancreatic Insufficiency / drug therapy*, enzymology Humans Lipase / analysis, antagonists & inhibitors* Pancreatic Juice / analysis, secretion Pancreatin / administration & dosage, therapeutic use* Pancreatitis / drug therapy*, enzymology Secretin / analysis Trypsin / analysis |
Chemical | |
Reg. No./Substance:
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1393-25-5/Secretin; 8049-47-6/Pancreatin; EC 3.1.1.3/Lipase; EC 3.2.1.-/Amylases; EC 3.4.21.4/Trypsin |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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