Short-chain lecithin long-chain phospholipid unilamellar vesicles: asymmetry, dynamics, and enzymatic hydrolysis of the short-chain component

Biochemistry ◽  
1987 ◽  
Vol 26 (9) ◽  
pp. 2432-2440 ◽  
Author(s):  
N. Elise Gabriel ◽  
Mary F. Roberts
Keyword(s):  
Enzymatic Hydrolysis ◽  
Short Chain ◽  
Unilamellar Vesicles ◽  
Chain Component ◽  
Hydrolysis Of ◽  
Long Chain

scholarly journals Partial purification of a diacylglycerol lipase from bovine aorta

1994 ◽  
Vol 298 (1) ◽  
pp. 213-219 ◽  
Author(s):  
M W Lee ◽  
D L Severson
Keyword(s):  
Lipase Activity ◽  
Specific Activity ◽  
Competitive Inhibitor ◽  
Short Chain ◽  
Partial Purification ◽  
Diacylglycerol Lipase ◽  
Bivalent Cations ◽  
Triton X ◽  
Hydrolysis Of ◽  
Long Chain

A diacylglycerol (DG) lipase has been purified from a soluble subcellular fraction of bovine aorta by (NH4)2SO4 precipitation in the presence of 5.0% (w/v) Triton X-100, followed by chromatography on DEAE-Sephacel, heparin-Sepharose and octyl-Sepharose in the presence of either CHAPS or Triton X-100 detergents. Under basal conditions, the hydrolysis of a short-chain [3H]dioctanoylglycerol ([3H]diC8) substrate was much greater than that of a long-chain 1-[1-14C]palmitoyl-2-oleoyl-sn-glycerol (1-[14C]POG) substrate. Lipase activity measured with 1-[14C]POG was markedly enhanced by Triton X-100. In the presence of 0.1% Triton X-100, specific enzyme activities in the octyl-Sepharose fraction determined with 1-[14C]POG or 1-stearoyl-2-[1-14C]-arachidonoyl-sn-glycerol as substrates were the same as that measured with [3H]diC8. MgCl2 (5mM) or CaCl2 (2 mM) also selectively stimulated lipase activity (up to 10-13-fold) measured with the long-chain (1-[14C]POG) substrate only. The increase in relative specific activity in the octyl-Sepharose fraction was 60-fold and 155-fold, based on hydrolysis of [3H]diC8 and 1-[14C]POG (+ Triton X-100), respectively. Unlabelled diC8 was a competitive inhibitor of 1-[14C]POG hydrolysis, suggesting that a single lipase hydrolyses both the short-chain and long-chain DG substrates; selective stimulatory effects of non-ionic detergents and bivalent cations on the hydrolysis of 1-[14C]POG may be due to effects on the physical properties of the substrate preparation. Monoacylglycerol lipase, DG kinase and cholesterol esterase activities could not be detected in the partially purified lipase preparation.

Determining the substrate permeability through the bilayer of large unilamellar vesicles of DOPC. A kinetic study

RSC Advances ◽  
2016 ◽  
Vol 6 (67) ◽  
pp. 62594-62601 ◽  
Author(s):  
Maria Alejandra Luna ◽  
Juana J. Silber ◽  
Leonides Sereno ◽  
N. Mariano Correa ◽  
Fernando Moyano
Keyword(s):  
Enzymatic Hydrolysis ◽  
Kinetic Study ◽  
Unilamellar Vesicles ◽  
Large Unilamellar Vesicles ◽  
Hydrolysis Of

In this work we determine the permeability of DOPC vesicles in the presence of different cholesterol contents, by using the enzymatic hydrolysis of N-benzoyl-l-tyrosine p-nitroanilide catalyzed by α-chymotrypsin.

scholarly journals Characterization and purification of neutrophil ecto-phosphatidic acid phosphohydrolase

1997 ◽  
Vol 324 (3) ◽  
pp. 941-950 ◽  
Author(s):  
Denis ENGLISH ◽  
Margaret MARTIN ◽  
Kevin A. HARVEY ◽  
Luke P. AKARD ◽  
Ruth ALLEN ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Phosphatidic Acid ◽  
Molecular Mass ◽  
Biological Systems ◽  
Short Chain ◽  
Intact Cells ◽  
Ability To Act ◽  
Phosphatidic Acids ◽  
Hydrolysis Of ◽  
Long Chain

Phosphatidic acid and its derivatives play potentially important roles as extracellular messengers in biological systems. An ecto-phosphatidic acid phosphohydrolase (ecto-PAPase) has been identified which effectively regulates neutrophil responses to exogenous phosphatidic acid by converting the substrate to diacylglycerol. The present study was undertaken to characterize this ecto-enzyme on intact cells and to isolate the enzyme from solubilized neutrophil extracts. In the absence of detergent, short chain phosphatidic acids were hydrolysed most effectively by neutrophil plasma membrane ecto-PAPase; both saturated and unsaturated long chain phosphatidic acids were relatively resistant to hydrolysis. Both long (C18:1) and short (C8) chain lyso-phosphatidic acids were hydrolysed at rates comparable with those observed for short chain (diC8) phosphatidic acid. Activity of the ecto-enzyme accounted for essentially all of the N-ethylmaleimide-insensitive, Mg2+-independent PAPase activity recovered from disrupted neutrophils. At 37 °C and pH 7.2, the apparent Km for dioctanoyl phosphatidic acid (diC8PA) was 1.4×10-3 M. Other phosphatidic acids and lysophosphatidic acids inhibited hydrolysis of [32P]diC8PA in a rank order that correlated with competitor solubility, lysophosphatidic acids and unsaturated phosphatidic acids being much more effective inhibitors than long chain saturated phosphatidic acids. Dioleoyl (C18:1) phosphatidic acid was an unexpectedly strong inhibitor of activity, in comparison with its ability to act as a direct substrate in the absence of detergent. Other inhibitors of neutrophil ecto-PAPase included sphingosine, dimethyl- and dihydro-sphingosine, propranolol, NaF and MgCl2. Of several leucocyte populations isolated from human blood by FACS, including T cells, B cells, NK lymphocytes and monocytes, ecto-PAPase was most prevalent on neutrophils; erythrocytes were essentially devoid of activity. A non-hydrolysable, phosphonate analogue of phosphatidic acid, phosphonate 1, efficiently solubilized catalytic activity from intact neutrophils without causing cell disruption or increasing permeability. Enzyme activity in solubilized extracts was purified in the absence of detergent by successive heparin–Sepharose, gel filtration and anion exchange chromatography. By assaying activity in renatured SDS/polyacrylamide gel slices, the molecular mass of neutrophil ecto-PAPase was estimated to be between 45 and 52 kDa, similar to the molecular mass of previously purified plasma membrane PAPases. Since a large portion of neutrophil plasma membrane PAPase is available for hydrolysis of exogenous substrates, ecto-PAPase may play an important role in regulating inflammatory cell responses to extracellular phosphatidic acid in biological systems.

Improving Rheology and Enzymatic Hydrolysis of High-Solid Corncob Slurries by Adding Lignosulfonate and Long-Chain Fatty Alcohols

2014 ◽  
Vol 62 (33) ◽  
pp. 8430-8436 ◽  
Author(s):  
Hongming Lou ◽  
Shun Wu ◽  
Xiuli Li ◽  
Tianqing Lan ◽  
Dongjie Yang ◽  
...  
Keyword(s):  
Enzymatic Hydrolysis ◽  
Fatty Alcohols ◽  
High Solid ◽  
Hydrolysis Of ◽  
Long Chain

Enhancing enzymatic hydrolysis of xylan by adding sodium lignosulfonate and long-chain fatty alcohols

2016 ◽  
Vol 200 ◽  
pp. 48-54 ◽  
Author(s):  
Hongming Lou ◽  
Long Yuan ◽  
Xueqing Qiu ◽  
Kexian Qiu ◽  
Jinguo Fu ◽  
...  
Keyword(s):  
Enzymatic Hydrolysis ◽  
Fatty Alcohols ◽  
Sodium Lignosulfonate ◽  
Hydrolysis Of ◽  
Long Chain

Enzymatic Hydrolysis of Long-Chain Alkanoylcholines in Rat Intestinal Loops

1995 ◽  
Vol 30 (7) ◽  
pp. 670-674 ◽  
Author(s):  
M. Chelminska-Bertilsson ◽  
A. Edebo ◽  
R. A. Thompson ◽  
L. Edebo
Keyword(s):  
Enzymatic Hydrolysis ◽  
Hydrolysis Of ◽  
Long Chain

Enhancing enzymatic hydrolysis of crystalline cellulose and lignocellulose by adding long-chain fatty alcohols

Cellulose ◽  
2014 ◽  
Vol 21 (5) ◽  
pp. 3361-3369 ◽  
Author(s):  
Hongming Lou ◽  
Huanran Lai ◽  
Shun Wu ◽  
Xiuli Li ◽  
Dongjie Yang ◽  
...  
Keyword(s):  
Enzymatic Hydrolysis ◽  
Fatty Alcohols ◽  
Crystalline Cellulose ◽  
Hydrolysis Of ◽  
Long Chain

Microwave-assisted enzymatic hydrolysis of starch

2009 ◽  
Author(s):  
Marcin Lukasiewicz ◽  
Anna Osowiec ◽  
Magdalena Marciniak
Keyword(s):  
Enzymatic Hydrolysis ◽  
Microwave Assisted ◽  
Hydrolysis Of
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