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Product activation of pancreatic lipase. Lipolytic enzymes as probes for lipid/water interfaces

Wieloch, T. LU ; Borgstrom, B. ; Pieroni, G. ; Pattus, F. and Verger, R. (1982) In Journal of Biological Chemistry 257(19). p.11523-11528
Abstract

During the action of pancreatic lipase and colipase on racemic 1,2-didodecanoylglycerol monolayers in the absence of bile salts, biphasic kinetics was observed under conditions of high lipid packing. Similar kinetics has earlier been reported using phospholipid-emulsified triolein droplets. These kinetics are characterized by a lag time τ(d), dependent on products accumulation at the substrate/water interface. This lag time is differentiated from the previously described enzyme concentration independent lag time τ(i) in systems of low lipid packing. Both τ(i) and τ(d) reflect a rate-limiting step due to the slow enzyme penetration into the substrate interface. The variation of τ(d) under different conditions (change in pH and... (More)

During the action of pancreatic lipase and colipase on racemic 1,2-didodecanoylglycerol monolayers in the absence of bile salts, biphasic kinetics was observed under conditions of high lipid packing. Similar kinetics has earlier been reported using phospholipid-emulsified triolein droplets. These kinetics are characterized by a lag time τ(d), dependent on products accumulation at the substrate/water interface. This lag time is differentiated from the previously described enzyme concentration independent lag time τ(i) in systems of low lipid packing. Both τ(i) and τ(d) reflect a rate-limiting step due to the slow enzyme penetration into the substrate interface. The variation of τ(d) under different conditions (change in pH and concentration of Ca2+, enzyme, bovine serum albumin, and lipolytic products) lead us to propose a model for the product activation during lipolysis. We will discuss the use of the pancreatic lipase-colipase system to probe the lipid packing of emulsified triglyceride particles and lipoproteins using τ(d) as a reference value.

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organization
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type
Contribution to journal
publication status
published
subject
in
Journal of Biological Chemistry
volume
257
issue
19
pages
6 pages
publisher
ASBMB
external identifiers
  • pmid:7118893
  • scopus:0020373352
ISSN
0021-9258
language
English
LU publication?
yes
id
cb957714-4d9b-4ff9-952b-369e9312c8bf
alternative location
http://www.jbc.org/content/257/19/11523.abstract
date added to LUP
2019-06-13 17:51:04
date last changed
2020-10-25 06:26:42
@article{cb957714-4d9b-4ff9-952b-369e9312c8bf,
  abstract     = {<p>During the action of pancreatic lipase and colipase on racemic 1,2-didodecanoylglycerol monolayers in the absence of bile salts, biphasic kinetics was observed under conditions of high lipid packing. Similar kinetics has earlier been reported using phospholipid-emulsified triolein droplets. These kinetics are characterized by a lag time τ(d), dependent on products accumulation at the substrate/water interface. This lag time is differentiated from the previously described enzyme concentration independent lag time τ(i) in systems of low lipid packing. Both τ(i) and τ(d) reflect a rate-limiting step due to the slow enzyme penetration into the substrate interface. The variation of τ(d) under different conditions (change in pH and concentration of Ca<sup>2+</sup>, enzyme, bovine serum albumin, and lipolytic products) lead us to propose a model for the product activation during lipolysis. We will discuss the use of the pancreatic lipase-colipase system to probe the lipid packing of emulsified triglyceride particles and lipoproteins using τ(d) as a reference value.</p>},
  author       = {Wieloch, T. and Borgstrom, B. and Pieroni, G. and Pattus, F. and Verger, R.},
  issn         = {0021-9258},
  language     = {eng},
  month        = {12},
  number       = {19},
  pages        = {11523--11528},
  publisher    = {ASBMB},
  series       = {Journal of Biological Chemistry},
  title        = {Product activation of pancreatic lipase. Lipolytic enzymes as probes for lipid/water interfaces},
  url          = {http://www.jbc.org/content/257/19/11523.abstract},
  volume       = {257},
  year         = {1982},
}