Change search
ReferencesLink to record
Permanent link

Direct link
Bovine pregastric lipase: a model for the human enzyme with respect to properties relevant to its site of action.
Umeå University, Faculty of Medicine, Department of Clinical Sciences, Paediatrics.
1987 (English)In: Biochimica et Biophysica Acta, ISSN 0006-3002, Vol. 922, no 2, 206-13 p.Article in journal (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
1987. Vol. 922, no 2, 206-13 p.
URN: urn:nbn:se:umu:diva-45454PubMedID: 3676343OAI: diva2:429474
Available from: 2011-07-04 Created: 2011-07-04 Last updated: 2011-07-04

Open Access in DiVA

No full text


Search in DiVA

By author/editor
Hernell, Olle
By organisation
In the same journal
Biochimica et Biophysica Acta

Search outside of DiVA

GoogleGoogle Scholar
The number of downloads is the sum of all downloads of full texts. It may include eg previous versions that are now no longer available

Altmetric score

Total: 33 hits
ReferencesLink to record
Permanent link

Direct link