Linked Life Data

16154275

Source:http://linkedlifedata.com/resource/pubmed/id/16154275

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2005-10-28
pubmed:abstractText
Higher animal's lipases are well characterized, however, much less is known about lipases from primitive ones. We choose the scorpion, one of the most ancient invertebrates, as a model of a primitive animal. A lipolytic activity was located in the scorpion digestive glands, from which a scorpion digestive lipase (SDL) was purified. Pure SDL, a glycosylated protein, has a molecular mass of 50 kDa, it presents the interfacial activation phenomenon. It was found to be more active on short-chain triacylglycerols than on long-chain triacylglycerols. SDL is a serine enzyme and possesses one accessible sulfhydryl group which is not essential for the catalysis. Among the NH2-terminal 33 residues, a 17 amino acids sequence shows similarities with sequence of Drosophila melanogaster putative lipase. Interestingly, neither colipase, nor bile salts were detected in the scorpion hepatopancreas. This indicates that colipase evolved in vertebrates simultaneously with the appearance of an exocrine pancreas and a true liver which produces bile salts. Furthermore, polyclonal antibodies directed against SDL failed to recognise the classical digestive lipases. Altogether, these results suggest that SDL is a member of a new group of digestive lipases belonging to invertebrates.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
30
pubmed:volume
1726
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
67-74
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Purification and characterization of a novel lipase from the digestive glands of a primitive animal: the scorpion.
pubmed:affiliation
Laboratoire de Biochimie et de Génie Enzymatique des Lipases, ENIS, BPW route de Soukra, 3038 Sfax, Tunisia.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't