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1.
Biochim Biophys Acta ; 1791(12): 1125-32, 2009 Dec.
Artigo em Inglês | MEDLINE | ID: mdl-19635584

RESUMO

Whereas hepatocytes secrete the major human plasma high density lipoproteins (HDL)-protein, apo A-I, as lipid-free and lipidated species, the biogenic itineraries of apo A-II and apo E are unknown. Human plasma and HepG2 cell-derived apo A-II and apo E occur as monomers, homodimers and heterodimers. Dimerization of apo A-II, which is more lipophilic than apo A-I, is catalyzed by lipid surfaces. Thus, we hypothesized that lipidation of intracellular and secreted apo A-II exceeds that of apo A-I, and once lipidated, apo A-II dimerizes. Fractionation of HepG2 cell lysate and media by size exclusion chromatography showed that intracellular apo A-II and apo E are fully lipidated and occur on nascent HDL and VLDL respectively, while only 45% of intracellular apo A-I is lipidated. Secreted apo A-II and apo E occur on small HDL and on LDL and large HDL respectively. HDL particles containing both apo A-II and apo A-I form only after secretion from both HepG2 and Huh7 hepatoma cells. Apo A-II dimerizes intracellularly while intracellular apo E is monomeric but after secretion associates with HDL and subsequently dimerizes. Thus, HDL apolipoproteins A-I, A-II and E have distinct intracellular and post-secretory pathways of hepatic lipidation and dimerization in the process of HDL formation. These early forms of HDL are expected to follow different apolipoprotein-specific pathways through plasma remodeling and reverse cholesterol transport.


Assuntos
Apolipoproteína A-II/metabolismo , Apolipoproteína A-I/metabolismo , Apolipoproteínas E/metabolismo , Carcinoma Hepatocelular/metabolismo , Espaço Intracelular/metabolismo , Lipoproteínas HDL/metabolismo , Neoplasias Hepáticas/metabolismo , Cromatografia em Gel , Células Hep G2 , Humanos , Modelos Biológicos , Ligação Proteica , Multimerização Proteica , Sefarose/análogos & derivados , Fatores de Tempo , Ultracentrifugação
2.
Biochim Biophys Acta ; 1781(5): 245-53, 2008 May.
Artigo em Inglês | MEDLINE | ID: mdl-18406360

RESUMO

Formation of discoidal high density lipoproteins (rHDL) by apolipoprotein A-I (apoA-I) mediated solubilization of dimyristoyl phosphatidylcholine (DMPC) multilamellar vesicles (MLV) was dramatically affected by bilayer cholesterol concentration. At a low ratio of DMPC/apoA-I (2 mg DMPC/mg apoA-I, 84/1 mol/mol), sterols (cholesterol, lathosterol, and beta-sitosterol) that form ordered lipid phases increase the rate of solubilization similarly, yielding rHDL with similar structures. By changing the temperature and sterol concentration, the rates of solubilization varied almost 3 orders of magnitude; however, the sizes of the rHDL were independent of the rate of their formation and dependent upon the bilayer sterol concentration. At a high ratio of DMPC/apoA-I (10/1 mg DMPC/mg apoA-I, 420/1 mol/mol), changing the temperature and cholesterol concentration yielded rHDL that varied greatly in size, phospholipid/protein ratio, mol% cholesterol, and number of apoA-I molecules per particle. rHDL were isolated that had 2, 4, 6, and 8 molecules of apoA-I per particle, mean diameters of 117, 200, 303, and 396 A, and a mol% cholesterol that was similar to the original MLV. Kinetic studies demonstrated that the different sized rHDL are formed independently and concurrently. The rate of formation, lipid composition, and three-dimensional structures of cholesterol-rich rHDL is dictated primarily by the original membrane phase properties and cholesterol content. The size speciation of rHDL and probably nascent HDL formed via the activity of the ABCA1 lipid transporter is mechanistically linked to the cholesterol content of the membranes from which they were formed.


Assuntos
Apolipoproteína A-I/química , Colesterol/metabolismo , Lipoproteínas HDL/química , Membranas/química , Apolipoproteína A-I/metabolismo , Dimiristoilfosfatidilcolina/química , Humanos , Indicadores e Reagentes/química , Lipoproteínas HDL/metabolismo , Lipoproteínas HDL/ultraestrutura , Tamanho da Partícula , Fosfolipídeos/química , Solubilidade
3.
J Lipid Res ; 50(6): 1229-36, 2009 Jun.
Artigo em Inglês | MEDLINE | ID: mdl-19179308

RESUMO

Plasma HDL-cholesterol and apolipoprotein A-I (apoA-I) levels are strongly inversely associated with cardiovascular disease. However, the structure and protein composition of HDL particles is complex, as native and synthetic discoidal and spherical HDL particles can have from two to five apoA-I molecules per particle. To fully understand structure-function relationships of HDL, a method is required that is capable of directly determining the number of apolipoprotein molecules in heterogeneous HDL particles. Chemical cross-linking followed by SDS polyacrylamide gradient gel electrophoresis has been previously used to determine apolipoprotein stoichiometry in HDL particles. However, this method yields ambiguous results due to effects of cross-linking on protein conformation and, subsequently, its migration pattern on the gel. Here, we describe a new method based on cross-linking chemistry followed by MALDI mass spectrometry that determines the absolute mass of the cross-linked complex, thereby correctly determining the number of apolipoprotein molecules in a given HDL particle. Using well-defined, homogeneous, reconstituted apoA-I-containing HDL, apoA-IV-containing HDL, as well as apoA-I/apoA-II-containing HDL, we have validated this method. The method has the capability to determine the molecular ratio and molecular composition of apolipoprotein molecules in complex reconstituted HDL particles.


Assuntos
Apolipoproteínas/análise , Lipoproteínas HDL/química , Espectrometria de Massas por Ionização e Dessorção a Laser Assistida por Matriz/métodos , Apolipoproteína A-I/análise , Apolipoproteína A-I/sangue , Apolipoproteína A-II/análise , Apolipoproteína A-II/sangue , Apolipoproteínas/sangue , Apolipoproteínas/química , Apolipoproteínas A/análise , Apolipoproteínas A/sangue , Análise Química do Sangue/métodos , Eletroforese das Proteínas Sanguíneas/métodos , Reagentes de Ligações Cruzadas , Dimiristoilfosfatidilcolina , Eletroforese em Gel de Poliacrilamida , Humanos , Técnicas In Vitro , Lipoproteínas HDL/sangue , Lipossomos , Fosfatidilcolinas
4.
Chem Phys Lipids ; 156(1-2): 45-51, 2008 Nov.
Artigo em Inglês | MEDLINE | ID: mdl-18838065

RESUMO

Serum opacity factor from Streptococcus pyogenes transfers the cholesteryl esters (CE) of approximately 100,000 plasma high-density lipoprotein particles (HDL) to a CE-rich microemulsion (CERM) while forming neo HDL, a cholesterol-poor HDL-like particle. HDL, neo HDL, and CERM are distinct. Neo HDL is lower in free cholesterol and has lower surface and total microviscosities than HDL; the surface polarity of neo HDL and HDL are similar. CERM is much larger than HDL and richer in cholesterol and CE. Although the surface microviscosity of HDL is higher than that of CERM, they have similar total microviscosities because cholesterol partitions into the neutral lipid core. Because of its unique surface properties apo E preferentially associates with the CERM. In contrast, the composition and properties of neo HDL make it a potential acceptor of cellular cholesterol and its esterification. Thus, neo HDL and CERM are possible vehicles for improving cholesterol transport to the liver.


Assuntos
Ésteres do Colesterol/química , Lipoproteínas HDL/química , Peptídeo Hidrolases/metabolismo , Ésteres do Colesterol/isolamento & purificação , Ésteres do Colesterol/metabolismo , Cromatografia em Gel/métodos , Humanos , Lipoproteínas HDL/isolamento & purificação , Lipoproteínas HDL/metabolismo , Fígado/metabolismo , Fosfolipídeos/química , Espectrometria de Fluorescência , Propriedades de Superfície , Viscosidade
5.
Biochemistry ; 46(45): 12968-78, 2007 Nov 13.
Artigo em Inglês | MEDLINE | ID: mdl-17941651

RESUMO

Human plasma high-density lipoproteins (HDL) are important vehicles in reverse cholesterol transport, the cardioprotective mechanism by which peripheral tissue-cholesterol is transported to the liver for disposal. HDL is the target of serum opacity factor (SOF), a substance produced by Streptococcus pyogenes that turns mammalian serum cloudy. Using a recombinant (r) SOF, we studied opacification and its mechanism. rSOF catalyzes the partial disproportionation of HDL into a cholesteryl ester-rich microemulsion (CERM) and a new HDL-like particle, neo HDL, with the concomitant release of lipid-free (LF)-apo A-I. Opacification is unique; rSOF transfers apo E and nearly all neutral lipids of approximately 100,000 HDL particles into a single large CERM whose size increases with HDL-CE content (r approximately 100-250 nm) leaving a neo HDL that is enriched in PL (41%) and protein (48%), especially apo A-II. rSOF is potent; within 30 min at 37 degrees C, 10 nM rSOF opacifies 4 microM HDL. At respective low and high physiological HDL concentrations, LF-apo A-I is monomeric and tetrameric. CERM formation and apo A-I release have similar kinetics suggesting parallel or rapid sequential steps. According to the reaction products and kinetics, rSOF is a heterodivalent fusogenic protein that uses a docking site to displace apo A-I and bind to exposed CE surfaces on HDL; the resulting rSOF-HDL complex recruits additional HDL with its binding-delipidation site and through multiple fusion steps forms a CERM. rSOF may be a clinically useful and novel modality for improving reverse cholesterol transport. With apo E and a high CE content, CERM could transfer large amounts of cholesterol to the liver for disposal via the LDL receptor; neo HDL is likely a better acceptor of cellular cholesterol than HDL; LF-apo A-I could enhance efflux via the ATP-binding casette transporter ABCA1.


Assuntos
Apolipoproteína A-I/química , Lipoproteínas HDL/efeitos dos fármacos , Peptídeo Hidrolases/farmacologia , Humanos , Cinética , Proteínas Recombinantes/farmacologia
6.
Biochemistry ; 46(25): 7449-59, 2007 Jun 26.
Artigo em Inglês | MEDLINE | ID: mdl-17530866

RESUMO

The distribution of apolipoprotein (apo) A-I between human high-density lipoproteins (HDL) and water is an important component of reverse cholesterol transport and the atheroprotective effects of HDL. Chaotropic perturbation (CP) with guanidinium chloride (Gdm-Cl) reveals HDL instability by inducing the unfolding and transfer of apo A-I but not apo A-II into the aqueous phase while forming larger apo A-I deficient HDL-like particles and small amounts of cholesteryl ester-rich microemulsions (CERMs). Our kinetic and hydrodynamic studies of the CP of HDL species separated according to size and density show that (1) CP mediated an increase in HDL size, which involves quasi-fusion of surface and core lipids, and release of lipid-free apo A-I (these processes correlate linearly), (2) >94% of the HDL lipids remain with an apo A-I deficient particle, (3) apo A-II remains associated with a very stable HDL-like particle even at high levels of Gdm-Cl, and (4) apo A-I unfolding and transfer from HDL to water vary among HDL subfractions with the larger and more buoyant species exhibiting greater stability. Our data indicate that apo A-I's on small HDL (HDL-S) are highly dynamic and, relative to apo A-I on the larger more mature HDL, partition more readily into the aqueous phase, where they initiate the formation of new HDL species. Our data suggest that the greater instability of HDL-S generates free apo A-I and an apo A-I deficient HDL-S that readily fuses with the more stable HDL-L. Thus, the presence of HDL-L drives the CP remodeling of HDL to an equilibrium with even larger HDL-L and more lipid-free apo A-I than with either HDL-L or HDL-S alone. Moreover, according to dilution studies of HDL in 3 M Gdm-Cl, CP of HDL fits a model of apo A-I partitioning between HDL phospholipids and water that is controlled by the principal of opposing forces. These findings suggest that the size and relative amount of HDL lipid determine the HDL stability and the fraction of apo A-I that partitions into the aqueous phase where it is destined for interaction with ABCA1 transporters, thereby initiating reverse cholesterol transport or, alternatively, renal clearance.


Assuntos
Apolipoproteína A-I/sangue , Lipoproteínas HDL/sangue , Apolipoproteína A-I/metabolismo , Apolipoproteína A-II/sangue , Cromatografia em Gel , Dicroísmo Circular , Relação Dose-Resposta a Droga , Guanidina/farmacologia , Humanos , Cinética , Lipoproteínas HDL/isolamento & purificação , Modelos Biológicos , Peso Molecular , Água/química
7.
J Lipid Res ; 48(2): 348-57, 2007 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-17102149

RESUMO

Small, dense, electronegative low density lipoprotein [LDL(-)] is increased in patients with familial hypercholesterolemia and diabetes, populations at increased risk for coronary artery disease. It is present to a lesser extent in normolipidemic subjects. The mechanistic link between small, dense LDL(-) and atherogenesis is not known. To begin to address this, we studied the composition and dynamics of small, dense LDL(-) from normolipidemic subjects. NEFA levels, which correlate with triglyceride content, are quantitatively linked to LDL electronegativity. Oxidized LDL is not specific to small, dense LDL(-) or lipoprotein [a] (i.e., abnormal lipoprotein). Apolipoprotein C-III is excluded from the most abundant LDL (i.e., that of intermediate density: 1.034 < d < 1.050 g/ml) but associated with both small and large LDL(-). In contrast, lipoprotein-associated phospholipase A(2) (LpPLA(2)) is highly enriched only in small, dense LDL(-). The association of LpPLA(2) with LDL may occur through amphipathic helical domains that are displaced from the LDL surface by contraction of the neutral lipid core.


Assuntos
Lipoproteínas LDL/química , Lipoproteínas LDL/metabolismo , Fosfolipases A2/metabolismo , Apolipoproteína C-III/análise , Eletroquímica , Eletroforese em Gel de Poliacrilamida , Ácidos Graxos não Esterificados/química , Humanos , Lipoproteínas HDL/química , Lipoproteínas HDL/metabolismo , Oxirredução , Ligação Proteica , Eletricidade Estática
8.
Curr Opin Lipidol ; 17(3): 296-301, 2006 Jun.
Artigo em Inglês | MEDLINE | ID: mdl-16680036

RESUMO

PURPOSE OF REVIEW: Oxysterols, oxidation products of cholesterol, mediate numerous and diverse biological processes. The objective of this review is to explain some of the biochemical and cell biological properties of oxysterols based on their membrane biophysical properties and their interaction with integral and peripheral membrane proteins. RECENT FINDINGS: According to their biophysical properties, which can be distinct from those of cholesterol, oxysterols can promote or inhibit the formation of membrane microdomains or lipid rafts. Oxysterols that inhibit raft formation are cytotoxic. The stereo-specific binding of cholesterol to sterol-sensing domains in cholesterol homeostatic pathways is not duplicated by oxysterols, and some oxysterols are poor substrates for the pathways that detoxify cells of excess cholesterol. The cytotoxic roles of oxysterols are, at least partly, due to a direct physical effect on membranes involved in cholesterol-induced cell apoptosis and raft mediated cell signaling. Oxysterols regulate cellular functions by binding to oxysterol binding protein and oxysterol binding protein-related proteins. Oxysterol binding protein is a sterol-dependent scaffolding protein that regulates the extracellular signal-regulated kinase signaling pathway. According to a recently solved structure for a yeast oxysterol binding protein-related protein, Osh4, some members of this large family of proteins are likely sterol transporters. SUMMARY: Given the association of some oxysterols with atherosclerosis, it is important to identify the mechanisms by which their association with cell membranes and intracellular proteins controls membrane structure and properties and intracellular signaling and metabolism. Studies on oxysterol binding protein and oxysterol binding protein-related proteins should lead to new understandings about sterol-regulated signal transduction and membrane trafficking pathways in cells.


Assuntos
Membrana Celular/metabolismo , Metabolismo dos Lipídeos , Proteínas/metabolismo , Esteróis/metabolismo , Animais , Humanos , Ligação Proteica
9.
Biochemistry ; 45(35): 10747-58, 2006 Sep 05.
Artigo em Inglês | MEDLINE | ID: mdl-16939227

RESUMO

Oxysterols, derivatives of cholesterol that contain a second oxygen moiety, are intermediates in cholesterol catabolism, regulators of lipid metabolism, and toxic sterols with proatherogenic effects. In model membranes, cholesterol and eight selected oxysterols were compared by fluorescence probe techniques that measure changes in bilayer order and phase behavior and by the formation of detergent-resistant membranes (DRM). The oxysterols were modified on the sterol nucleus or on the isooctyl side chain. The model membranes consisted of dipalmitoyl phosphatidylcholine (DPPC) and mixtures of dioleoyl phosphatidylcholine with DPPC and with sphingomyelin. The different oxysterols induced changes in membrane properties according to the differences in their structures. Whereas the effects of some oxysterols on membrane order, fluorescence probe microenvironment, and DRM formation were similar to those of cholesterol, others had little or no effect. An empirical correlation ranking the oxysterols by their ability to modify membrane biophysical properties when compared to cholesterol led to a significant structure/function relationship between the biophysical measurements and an important cellular phenomenon, apoptosis. 7beta-Hydroxycholesterol, which is the most cytotoxic of the eight selected oxysterols, was one of the least cholesterol-like with respect to modification of membrane properties. The results suggest that an underlying mechanism for oxysterol-induced apoptosis in cells, e.g., monocyte/macrophages, should include their biophysical effects on membranes, such as the regulation of the formation and composition of sterol-rich membrane domains.


Assuntos
1,2-Dipalmitoilfosfatidilcolina/química , Membrana Celular/química , Colesterol/química , Fosfatidilcolinas/química , Fosfolipídeos/química , Esfingomielinas/química , Polarização de Fluorescência , Bicamadas Lipídicas/química , Microscopia de Fluorescência , Modelos Biológicos , Estrutura Molecular , Octoxinol/química , Solubilidade
10.
Biochemistry ; 44(30): 10423-33, 2005 Aug 02.
Artigo em Inglês | MEDLINE | ID: mdl-16042420

RESUMO

7-Ketocholesterol is an oxidized derivative of cholesterol with numerous physiological effects. In model membranes, 7-ketocholesterol and cholesterol were compared by physical measures of bilayer order and polarity, formation of detergent resistant domains (DRM), phase separation, and membrane microsolubilization by apolipoprotein A-I. In binary mixtures of a saturated phosphatidylcholine (PC), dipalmitoyl-PC (DPPC), and cholesterol or 7-ketocholesterol, the sterols modulate bilayer order and polarity and induce DRM formation to a similar extent. Cholesterol induces formation of ordered lipid domains (rafts) in tertiary mixtures with dioleoyl-PC (DOPC) and DPPC, or DOPC and sphingomyelin (SM). In tertiary mixtures, cholesterol increased lipid order and reduces bilayer polarity more than 7-ketocholesterol. This effect was more pronounced when the mixtures were in a miscible liquid-disordered (L(d)) phase. Substitution of 7-ketocholesterol for cholesterol dramatically reduced the extent of DRM formation in DOPC/DPPC and DOPC/SM bilayers and ordered lipid phase separation in mixtures of a spin-labeled PC with DPPC and with SM. Compared to cholesterol, 7-ketocholesterol decreased the rate for the microsolubilization of dimyristoyl-PC multilamellar vesicles by apolipoprotein A-I. The membrane effects of 7-ketocholesterol were dependent on the phospholipid matrix. In L(d) phase phospholipids, a model for 7-ketocholesterol indicates that the proximity of the 7-keto and 3beta-OH groups puts both polar moieties at the lipid-water interface to tilt the sterol nucleus to the plane of the bilayer. 7-Ketocholesterol was less effective in forming ordered lipid domains, in decreasing the level of bilayer hydration, and in forming phase boundary bilayer defects. Compared to cholesterol, 7-ketocholesterol can differentially modulate membrane properties involved in protein-membrane association and function.


Assuntos
Apolipoproteína A-I/química , Cetocolesteróis/química , Microdomínios da Membrana/química , 1,2-Dipalmitoilfosfatidilcolina/química , HDL-Colesterol/química , Dimiristoilfosfatidilcolina/química , Humanos , Cetocolesteróis/metabolismo , Cinética , Bicamadas Lipídicas/química , Lipossomos , Microdomínios da Membrana/metabolismo , Octoxinol , Transição de Fase , Fosfatidilcolinas/química , Solubilidade , Espectrometria de Fluorescência , Esfingomielinas/química
11.
Biochemistry ; 44(43): 14376-84, 2005 Nov 01.
Artigo em Inglês | MEDLINE | ID: mdl-16245954

RESUMO

Oxygenated derivatives of cholesterol, oxysterols, have different physicochemical properties and three-dimensional shapes. The kinetics of microsolubilization of dimyristoylphosphatidylcholine (DMPC) multilamellar vesicles by apolipoprotein A-I (apoA-I) to form discoidal high-density lipoproteins (rHDL) was dramatically affected by oxysterol chemical structure. Under the experimental conditions of varying oxysterol chemical structure, sterol concentration, and the lipid phase state of DMPC, the kinetics varied over 3 orders of magnitude. Some oxysterols behaved similarly to cholesterol and increased the rate of microsolubilization; however, they were not as effective as cholesterol. Other oxysterols greatly inhibited this process. In general, there was no correlation of the rates with membrane fluidity as measured by fluorescence polarization. The rate of DMPC microsolubilization by apoA-I is highly dependent upon the presence of lattice defects in the membrane surface that occur due to imperfect packing of coexisting lipid phases. The differential ability of various oxysterols to induce the formation of an ordered lipid phase is the probable basis for their effects on the rates of DMPC microsolubilization. There was no effect of oxysterol chemical structure on the structure of the equilibrium rHDL products; however, there was a dramatic effect of sterol concentration on rHDL particle size. Different oxysterols regulate the kinetics of apoA-I membrane association by altering structural microheterogeneity at the membrane surface. However, once the kinetic barrier is overcome, the particle sizes of rHDL products formed are determined solely by the amount of sterol presence.


Assuntos
Apolipoproteína A-I/farmacologia , Colesterol/análogos & derivados , Compostos de Epóxi/química , Microdomínios da Membrana/efeitos dos fármacos , Fosfolipídeos/química , Colesterol/metabolismo , Eletroforese em Gel de Poliacrilamida , Compostos de Epóxi/metabolismo , Cinética , Lipoproteínas HDL/química , Lipoproteínas HDL/metabolismo , Microdomínios da Membrana/química , Microdomínios da Membrana/metabolismo , Microquímica , Tamanho da Partícula , Fosfolipídeos/metabolismo , Solubilidade , Temperatura
12.
Biochemistry ; 44(2): 471-9, 2005 Jan 18.
Artigo em Inglês | MEDLINE | ID: mdl-15641771

RESUMO

Although plasma high-density lipoproteins (HDL) have been implicated in several cardioprotective pathways, the physiologic role of apolipoprotein (apo) A-II, the second most abundant of the HDL proteins, remains ambiguous. Human apo A-II is distinguished from most other species by a single cysteine (Cys6), which forms a disulfide bond with other cysteine-containing apos. In human plasma, nearly all apo A-II occurs as disulfide-linked homodimers of 17.4 kDa. Although dimerization is an important determinant of human apo A-II metabolism, its mechanism and the plasma and/or cellular sites of its dimerization are not known. Using SDS-PAGE and densitometry we investigated the kinetics of apo A-II dimerization and observed a slow (t(1/2) = approximately 10 days), second-order process in Tris-buffered saline. In 3 M guanidine hydrochloride, which disrupts apo A-II secondary structure and self-association, the rate was 3-fold slower. In contrast, lipid surfaces that promote apo A-II alpha-helix formation and lipophilic interaction profoundly enhanced the rate. Reassembled HDL increased the second-order rate constant k(2) by 7500-fold, unilamellar 1-palmitoyl-2-oleoylphosphatidylcholine vesicles increased k(2) 850-fold, and physiological concentrations of human serum albumin increased k(2) 220-fold. Thus, while dimerization of apo A-II in aqueous buffer is too slow to account for the high fraction of dimer found in plasma, lipids and proteins "catalyze" dimer formation, a process that could occur either intracellularly prior to secretion or in the plasma compartment following secretion. These data suggest that formation of disulfide links within or between polypeptide chains can be controlled, in part, by coexisting lipids and proteins.


Assuntos
Apolipoproteína A-II/sangue , Apolipoproteína A-II/química , Proteínas de Transporte/sangue , Proteínas de Transporte/química , Dimerização , Dissulfetos/química , Guanidina/química , Humanos , Cinética , Bicamadas Lipídicas/química , Lipoproteínas HDL/sangue , Lipoproteínas HDL/química , Modelos Químicos , Fosfatidilcolinas/química , Desnaturação Proteica , Estrutura Secundária de Proteína , Albumina Sérica/química
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