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Titolo:
Hydrolysis of phospholipids by purified milk lipoprotein lipase - Effect of apoprotein CII, CIII, A and E, and synthetic fragments
Autore:
Lambert, DA; Smith, LC; Pownall, H; Sparrow, JT; Nicolas, JP; Gotto, AM;
Indirizzi:
Fac Med Vandoeuvre Nancy, INSERM, U308, F-54505 Vandoeuvre Nancy, France Fac Med Vandoeuvre Nancy Vandoeuvre Nancy France F-54505 e Nancy, France Baylor Coll Med, Dept Med, Houston, TX 77030 USA Baylor Coll Med Houston TX USA 77030 Med, Dept Med, Houston, TX 77030 USA
Titolo Testata:
CLINICA CHIMICA ACTA
fascicolo: 1, volume: 291, anno: 2000,
pagine: 19 - 33
SICI:
0009-8981(20000120)291:1<19:HOPBPM>2.0.ZU;2-V
Fonte:
ISI
Lingua:
ENG
Soggetto:
LOW-DENSITY LIPOPROTEINS; APOLIPOPROTEIN-C-II; HUMAN-PLASMA; CATALYTIC SITE; KINETICS; MECHANISM; HYPERTRIGLYCERIDEMIA; RECOMBINANTS; ACTIVATION; BINDING;
Keywords:
apolipoproteins; lipoprotein lipase; hyperlipoproteinemia; protein cofactors;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
40
Recensione:
Indirizzi per estratti:
Indirizzo: Lambert, DA Fac Med Vandoeuvre Nancy, INSERM, U308, BP 184 Ave de la Foretde Haye, F-54505 Vandoeuvre Nancy, France Fac Med Vandoeuvre Nancy BP 184 Ave de la Foret de Haye Vandoeuvre Nancy France F-54505
Citazione:
D.A. Lambert et al., "Hydrolysis of phospholipids by purified milk lipoprotein lipase - Effect of apoprotein CII, CIII, A and E, and synthetic fragments", CLIN CHIM A, 291(1), 2000, pp. 19-33

Abstract

Different pyrene-labeled phospholipid monolayer vesicles were used as substrates for the bovine milk lipoprotein lipase activity. The effects of synthetic fragments of apoprotein C II were measured on the hydrolysis of 1-myristoyl-2[9(1pyrenyl)-nonanoyl] phosphatidylcholine in vesicles: The activating capacity of fragments 30-78 and 43-78, 50-78 and 55-78, compared to entire apo CII, were similar to that, obtained with hydrolysable triglycerides. Our study shows that the longer the carboxy terminal fragment is, the higher is the activation. The phospholipid hydrolysis activity represents in the presence of apo C II, 36% of the triglycerides hydrolysis activity. Phospholipid hydrolysis is less dependent on activator than triglycerides hydrolysis (100% and 300% of increase with apo CII for phosphatidyl-choline and triglycerides respectively). The ratio hydrolysis without apo C II/hydrolysis with apo CII was different when other phospholipids than myrystoyl-phospatidylcholine were assayed: phosphatidyl-serine, ethanolamine, -choline, -glycerol, or diglycerides and butanoylglycerols. Fragment CIII1 (1-40) whichdid not bind to lipids, had no inhibitory effect. The entire sugar moiety and the first 40 amino acids are not required for the total inhibition of LPL. Inhibition was also obtained with Apo A I, A II,C I and fragments of apo E. (C) 2000 Elsevier Science B.V. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 06/04/20 alle ore 07:12:50