Linked Life Data

8656075

Source:http://linkedlifedata.com/resource/pubmed/id/8656075

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
1996-7-30
pubmed:abstractText
The pancreas contains three homologous proteins, colipase-dependent pancreatic lipase (PL) and two recently described pancreatic lipase-related proteins, PLRP1 and PLRP2. Rat (r) PLRP2 was first identified as a zymogen granule membrane protein, GP-3. Subsequently, we showed that rPLRP2 could cleave fatty acids from triglycerides, but the kinetic properties of rPLRP2 have not been further investigated. To further characterize rPLRP2, we expressed the recombinant enzyme in a baculovirus system, purified the secreted protein, and measured its kinetic properties. rPLRP2 had a broad pH optimum and the curve was similar to that of rPL. At pH 7.5, rPLRP2 cleaved short, medium, and long chain triglycerides by a kinetic mechanism that did not include interfacial activation. The activity against these substrates was not affected by bile salts. In particular, rPLRP2 did not show the bile salt inhibition typical of PL. Although colipase increased rPLRP2 activity in the presence of bile salts, the increase was only 2- to 5-fold compared to the absolute requirement for colipase that rPL had under these conditions. Finally, rPLRP2 could hydrolyze phospholipids, a substrate poorly hydrolyzed by PL. Our characterization of rPLRP2 demonstrates clear differences among the kinetic properties of rPLRP2 and rPL, rPLRP2, and PLRP2 homologues isolated from guinea pig and coypu pancreas. These findings have important implications for the physiological function of rPLRP2.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0022-2275
pubmed:author
pubmed:issnType
Print
pubmed:volume
36
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2374-82
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Rat GP-3 is a pancreatic lipase with kinetic properties that differ from colipase-dependent pancreatic lipase.
pubmed:affiliation
Department of Pediatrics, Washington University School of Medicine, St. Louis Children's Hospital, MO 63110, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't