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Hydrolysis of tri- and monoacylglycerol by lipoprotein lipase: evidence for a common active site

Twu, Jer-Shung; Nilsson-Ehle, Peter LU and Schotz, Michael C (1976) In Biochemistry 15(9). p.1904-1909
Abstract
The relationship between triacylglycerol and monoacylglycerol hydrolyzing activities of purified rat heart lipoprotein lipase was studied using emulsified trioleoylglycerol and micellar or albumin-bound monooleoylglycerol as substrates. The maximal reaction rates obtained with the two substrates were similar (650 and 550 nmol of fatty acid released per min per mg of protein, respectively). Addition of apolipoprotein C-II or serum increased the maximal reaction rate for the trioleolyglycerol hydrolyzing activity about four-fold, but had no effect on the monooleolyglycerol hydrolyzing activity. Hydolysis of the two substrates apparently takes place at the same active site of the enzyme since (1) mutual competitive inhibition between the... (More)
The relationship between triacylglycerol and monoacylglycerol hydrolyzing activities of purified rat heart lipoprotein lipase was studied using emulsified trioleoylglycerol and micellar or albumin-bound monooleoylglycerol as substrates. The maximal reaction rates obtained with the two substrates were similar (650 and 550 nmol of fatty acid released per min per mg of protein, respectively). Addition of apolipoprotein C-II or serum increased the maximal reaction rate for the trioleolyglycerol hydrolyzing activity about four-fold, but had no effect on the monooleolyglycerol hydrolyzing activity. Hydolysis of the two substrates apparently takes place at the same active site of the enzyme since (1) mutual competitive inhibition between the substrates could be demonstrated; (2) the rate of inactivation of enzymatic activity with the two substrates in 1.2 M NaCl was the same; (3) similar losses of hydrolytic activity with tri- and monooleoylglycerol were observed in the presence of low concentrations of n-butyl (p-nitrophenyl) carbamide; (4) inhibition of both hydrolytic activities by this compound could be prevented by prior exposure of lipoprotein lipase to either substrate. (Less)
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author
publishing date
type
Contribution to journal
publication status
published
subject
in
Biochemistry
volume
15
issue
9
pages
1904 - 1909
publisher
The American Chemical Society
external identifiers
  • pmid:1268200
  • scopus:0017130014
ISSN
0006-2960
language
English
LU publication?
no
id
3b7c55e0-dec4-4553-8685-a8b515eb3fd1 (old id 1102622)
date added to LUP
2008-08-14 11:50:53
date last changed
2017-07-30 03:43:29
@article{3b7c55e0-dec4-4553-8685-a8b515eb3fd1,
  abstract     = {The relationship between triacylglycerol and monoacylglycerol hydrolyzing activities of purified rat heart lipoprotein lipase was studied using emulsified trioleoylglycerol and micellar or albumin-bound monooleoylglycerol as substrates. The maximal reaction rates obtained with the two substrates were similar (650 and 550 nmol of fatty acid released per min per mg of protein, respectively). Addition of apolipoprotein C-II or serum increased the maximal reaction rate for the trioleolyglycerol hydrolyzing activity about four-fold, but had no effect on the monooleolyglycerol hydrolyzing activity. Hydolysis of the two substrates apparently takes place at the same active site of the enzyme since (1) mutual competitive inhibition between the substrates could be demonstrated; (2) the rate of inactivation of enzymatic activity with the two substrates in 1.2 M NaCl was the same; (3) similar losses of hydrolytic activity with tri- and monooleoylglycerol were observed in the presence of low concentrations of n-butyl (p-nitrophenyl) carbamide; (4) inhibition of both hydrolytic activities by this compound could be prevented by prior exposure of lipoprotein lipase to either substrate.},
  author       = {Twu, Jer-Shung and Nilsson-Ehle, Peter and Schotz, Michael C},
  issn         = {0006-2960},
  language     = {eng},
  number       = {9},
  pages        = {1904--1909},
  publisher    = {The American Chemical Society},
  series       = {Biochemistry},
  title        = {Hydrolysis of tri- and monoacylglycerol by lipoprotein lipase: evidence for a common active site},
  volume       = {15},
  year         = {1976},
}