Hydrolysis of tri- and monoacylglycerol by lipoprotein lipase: evidence for a common active site
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1102622
- author
- Twu, Jer-Shung ; Nilsson-Ehle, Peter LU and Schotz, Michael C
- publishing date
- 1976
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Biochemistry
- volume
- 15
- issue
- 9
- pages
- 1904 - 1909
- publisher
- The American Chemical Society (ACS)
- 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
- 2016-04-01 12:07:49
- date last changed
- 2021-01-03 04:21:40
@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 (ACS)}},
series = {{Biochemistry}},
title = {{Hydrolysis of tri- and monoacylglycerol by lipoprotein lipase: evidence for a common active site}},
volume = {{15}},
year = {{1976}},
}