Product activation of pancreatic lipase. Lipolytic enzymes as probes for lipid/water interfaces
(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.
(Less)
- author
- Wieloch, T. LU ; Borgstrom, B. ; Pieroni, G. ; Pattus, F. and Verger, R.
- organization
- publishing date
- 1982-12-01
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Biological Chemistry
- volume
- 257
- issue
- 19
- pages
- 6 pages
- publisher
- American Society for Biochemistry and Molecular Biology
- external identifiers
-
- scopus:0020373352
- pmid:7118893
- 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
- 2024-01-01 10:36:16
@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 = {{American Society for Biochemistry and Molecular Biology}},
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}},
}