Base de dados : MEDLINE
Pesquisa : D12.776.290 [Categoria DeCS]
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[PMID]:28465176
[Au] Autor:Nasabi M; Labbafi M; Mousavi ME; Madadlou A
[Ad] Endereço:Department of Food Science and Engineering, Razi Food Chemistry Lab, Faculty of Agricultural Engineering and Technology, University of Tehran, Karaj, Iran.
[Ti] Título:Effect of salts and nonionic surfactants on thermal characteristics of egg white proteins.
[So] Source:Int J Biol Macromol;102:970-976, 2017 Sep.
[Is] ISSN:1879-0003
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Effect of salts (Sodium chloride (NaCl), Sodium sulfate (Na SO ), Ammonium sulfate ((NH ) SO ), and nonionic surfactants (glycerol, tween20, tween80) on thermal properties of egg white proteins as a whole were investigated. Egg white solutions with additive (0, 0.5 and 1%) were collected after 0, 1 and 2min heat treatment. Physico-chemical properties of egg white proteins were evaluated by measuring heat coagulation time, solubility and turbidity of solution. Adding glycerol caused the most significant decrease in turbidity and increase in heat coagulation time and solubility of egg white, although Sodium Chloride had the least positive impact on physico-chemical properties of egg white under heat treatment. The Fourier transform infrared (FT-IR) spectroscopy analysis of heat treated egg white proteins as a whole with additives demonstrated changes in secondary protein structure, which are presented regarding the shape, intensity and position of FT-IR band. Meanwhile, it showed a good correlation with the physico-chemical properties consequences. Generally, the effect of nonionic surfactants were more noticeable than that of salts in preventing of egg white proteins aggregation under heat treatment. By improving thermal stability of egg white proteins, its usage in thermal processing industry can be evolved.
[Mh] Termos MeSH primário: Proteínas do Ovo/química
Sais/farmacologia
Tensoativos/farmacologia
Temperatura Ambiente
[Mh] Termos MeSH secundário: Animais
Agregados Proteicos/efeitos dos fármacos
Solubilidade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Egg Proteins); 0 (Protein Aggregates); 0 (Salts); 0 (Surface-Active Agents)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170504
[St] Status:MEDLINE


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[PMID]:29220173
[Au] Autor:Primacella M; Wang T; Acevedo NC
[Ad] Endereço:Department of Food Science and Human Nutrition, Iowa State University , 2312 Food Sciences Building, 536 Farm House Lane, Ames, Iowa 5011, United States.
[Ti] Título:Use of Reconstitued Yolk Systems To Study the Gelation Mechanism of Frozen-Thawed Hen Egg Yolk.
[So] Source:J Agric Food Chem;66(2):512-520, 2018 Jan 17.
[Is] ISSN:1520-5118
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Yolk gelation upon 5 week freezing-thawing was studied in four recombined yolk systems containing different plasma and granule proportions. Fractionation for mass distribution, sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) for protein distribution, and rheological properties were explored. Results indicate that both plasma and granule components, including low-density lipoprotein (LDL), high-density lipoprotein (HDL), and α-livetin proteins, contributed to gelation. Protein aggregation was reflected through a large mass increase in the granule fraction and appearance of a floating LDL layer upon fractionation of gelated yolk systems. A significant increase in gel strength (elastic modulus, G') was observed with the increase of the granule content. Overall, this study provides a better understanding of yolk gelation mechanism that may consequently lead to the design of innovative methods for preventing gelation. A schematic presentation of the yolk gelation mechanism is also proposed.
[Mh] Termos MeSH primário: Gema de Ovo/química
[Mh] Termos MeSH secundário: Animais
Galinhas
Proteínas do Ovo/química
Eletroforese em Gel de Poliacrilamida
Feminino
Géis/química
Lipoproteínas HDL/química
Lipoproteínas LDL/química
Peso Molecular
Reologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Egg Proteins); 0 (Gels); 0 (Lipoproteins, HDL); 0 (Lipoproteins, LDL); 9008-28-0 (livetin)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180205
[Lr] Data última revisão:
180205
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171209
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jafc.7b04370


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[PMID]:28873559
[Au] Autor:Pan D; Zhang D; Hao L; Lin S; Kang Q; Liu X; Lu L; Lu J
[Ad] Endereço:School of Life Sciences, Zhengzhou University, Zhengzhou, Henan, China.
[Ti] Título:Protective effects of soybean protein and egg white protein on the antibacterial activity of nisin in the presence of trypsin.
[So] Source:Food Chem;239:196-200, 2018 Jan 15.
[Is] ISSN:0308-8146
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The using of nisin to prevent foodborne pathogens (Staphylococcus aureus and Listeria monocytogenes) from contamination has received broad attentions during meat processing. However, the application of nisin has been limited because its antibacterial activity may be inhibited by trypsin. In this study, the protective effects of soybean protein and egg white protein on antibacterial activity of nisin were evaluated. It could be concluded that exogenous trypsin decreased the antibacterial activity of nisin, soybean protein and egg white protein could keep the nisin activity from enzymolysis of trypsin. Trypsin inhibitors in soybean protein and egg white protein could protect the antibacterial activity of nisin. Nisin with soybean protein or egg white protein in cooked meat product presented better quality preservation effects than nisin alone in the presence of trypsin. The total viable counts (TVC) and total volatile basic nitrogen (TVB-N) of nisin-treated group were significantly higher than these in nisin-soybean protein-treated and nisin-egg white protein-treated groups with trypsin. This study showed the potential of using soybean protein and egg white protein to stabilize the antibacterial activity of nisin under high trypsin conditions.
[Mh] Termos MeSH primário: Antibacterianos/farmacologia
[Mh] Termos MeSH secundário: Proteínas do Ovo
Listeria monocytogenes
Nisina
Proteínas de Soja
Staphylococcus aureus
Tripsina
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Egg Proteins); 0 (Soybean Proteins); 1414-45-5 (Nisin); EC 3.4.21.4 (Trypsin)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171128
[Lr] Data última revisão:
171128
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170907
[St] Status:MEDLINE


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[PMID]:28849994
[Au] Autor:Hultman MT; Petersen K; Tollefsen KE
[Ad] Endereço:a Norwegian Institute for Water Research (NIVA) , Oslo , Norway.
[Ti] Título:Characterizing combined effects of antiestrogenic chemicals on vitellogenin production in rainbow trout (Oncorhynchus mykiss) hepatocytes.
[So] Source:J Toxicol Environ Health A;80(16-18):987-1001, 2017.
[Is] ISSN:1528-7394
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Fish are exposed to a complex mixture of endocrine disrupting compounds (EDC), some of which display antiestrogenic activity leading to suppression of estrogen receptor (ER)- mediated reproductive processes. Although the main mode of action (MoA) of these antiestrogens is to directly interfere with natural ligand binding of the ER, several other MoA have been proposed. The aim of the present study was to characterize single and combined antiestrogenic effects of the aryl hydrocarbon receptor (AhR)-agonist ß-naphthoflavone (BNF) and ER-antagonist 4-hydroxytamoxifen (OHT) on vitellogenin (Vtg) protein using primary rainbow trout (Oncorhynchus mykiss) hepatocytes. Supporting transcriptional analysis of ER-responsive genes (estrogen receptor-α (er-α), vitellogenin-1 (vtg-1), eggshell zona radiata protein (zrp)) and AhR-mediated genes (aryl hydrocarbon receptor-2ß, cytochrome p450-1a (cyp1a)) was performed by qPCR to characterize the antiestrogenic influence on ER- and AhR-mediated responses. Data demonstrated that both BNF and OHT significantly reduced 17ß-estradiol (E2)-induced Vtg protein expression in a concentration responsive manner, whereas exposure to a mixture of these produced an additive antiestrogenic effect. The results observed at the protein level were further supported by transcriptional analysis of ER-responsive genes (er-α, vtg-1, zrp), where only E2-induced vtg-1 gene expression was significantly decreased by OHT and the mixture of OHT and BNF. E2-induced er-α and zrp gene expression was not markedly altered. The significant reduction of E2-induced vtg-1 gene expression by OHT suggested that the antiestrogenic effect of this compound may be associated with ER signaling pathway. Specific genes involved in putative AhR-ER cross-talk were also investigated, however none were directly associated with the compound anti-estrogenic MoA. Although the MoA of the single compounds and mixture were not completely characterized, the present study enhanced our knowledge of the combined toxicity mediated by antiestrogens acting through different MoA.
[Mh] Termos MeSH primário: Disruptores Endócrinos/toxicidade
Moduladores de Receptor Estrogênico/toxicidade
Hepatócitos/efeitos dos fármacos
Oncorhynchus mykiss/genética
Vitelogeninas/biossíntese
beta-Naftoflavona/toxicidade
[Mh] Termos MeSH secundário: Animais
Células Cultivadas
Citocromo P-450 CYP1A1/genética
Citocromo P-450 CYP1A1/metabolismo
Proteínas do Ovo/genética
Proteínas do Ovo/metabolismo
Estradiol/toxicidade
Receptor alfa de Estrogênio/genética
Receptor alfa de Estrogênio/metabolismo
Hepatócitos/metabolismo
Masculino
Oncorhynchus mykiss/metabolismo
Receptores de Hidrocarboneto Arílico/agonistas
Receptores de Hidrocarboneto Arílico/genética
Receptores de Hidrocarboneto Arílico/metabolismo
Receptores Estrogênicos/antagonistas & inibidores
Receptores Estrogênicos/genética
Receptores Estrogênicos/metabolismo
Transdução de Sinais
Tamoxifeno/análogos & derivados
Tamoxifeno/toxicidade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Egg Proteins); 0 (Endocrine Disruptors); 0 (Estrogen Receptor Modulators); 0 (Estrogen Receptor alpha); 0 (Receptors, Aryl Hydrocarbon); 0 (Receptors, Estrogen); 0 (Vitellogenins); 0 (zona radiata protein, fish); 094ZI81Y45 (Tamoxifen); 17197F0KYM (afimoxifene); 4TI98Z838E (Estradiol); 6051-87-2 (beta-Naphthoflavone); EC 1.14.14.1 (Cytochrome P-450 CYP1A1)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171031
[Lr] Data última revisão:
171031
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170830
[St] Status:MEDLINE
[do] DOI:10.1080/15287394.2017.1354435


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[PMID]:28813468
[Au] Autor:He T; Zhang H; Wang J; Wu S; Yue H; Qi G
[Ad] Endereço:Key Laboratory of Feed Biotechnology of Ministry of Agriculture, Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing, China.
[Ti] Título:Proteomic comparison by iTRAQ combined with mass spectrometry of egg white proteins in laying hens (Gallus gallus) fed with soybean meal and cottonseed meal.
[So] Source:PLoS One;12(8):e0182886, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cottonseed meal (CSM) is commonly used in hens' diets to replace soybean meal (SBM). However, the molecular consequences of this substitution remains unclear. To investigate the impact of this substitution at the molecular level, iTRAQ combined with biochemical analysis was performed in Hy-Line W-36 hens supplemented with a mixed diet of CSM and SBM. Egg weight, albumen height, and Haugh unit were significantly reduced in the CSM100 group (100% crude protein of SBM replaced by CSM) compared with the SBM group (P<0.05). A total of 15 proteins, accounting for 75% of egg white proteins with various biological functions of egg whites, were found to be reduced. This finding may relate to the decrease of albumen quality in the CSM100 group. Oviduct magnum morphology and hormone analysis indicated that a reduced level of plasma progesterone caused reduced growth of the tubular gland and epithelial cells in the magnum, further decreasing egg white protein synthesis in the magnum. These findings help demonstrate the molecular mechanisms of a CSM diet that cause adverse effects on albumen quality, while also showing that SBM should not be totally replaced with CSM in a hen diet.
[Mh] Termos MeSH primário: Galinhas/fisiologia
Óleo de Sementes de Algodão
Dieta/veterinária
Proteínas do Ovo/metabolismo
Espectrometria de Massas
Proteômica
Feijão de Soja
[Mh] Termos MeSH secundário: Animais
Eletroforese em Gel Bidimensional
Feminino
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cottonseed Oil); 0 (Egg Proteins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171013
[Lr] Data última revisão:
171013
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170817
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0182886


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[PMID]:28796944
[Au] Autor:Naderi N; Pouliot Y; House JD; Doyen A
[Ad] Endereço:Institute of Nutrition and Functional Foods (INAF), Department of Food Science, Université Laval , Québec, Québec G1V 0A6, Canada.
[Ti] Título:Effect of Freezing, Thermal Pasteurization, and Hydrostatic Pressure on Fractionation and Folate Recovery in Egg Yolk.
[So] Source:J Agric Food Chem;65(35):7774-7780, 2017 Sep 06.
[Is] ISSN:1520-5118
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In this study, the impact of pasteurization and freezing of raw material, as performed at a commercial scale, on egg yolk fractionation and folate recovery was assessed. Freezing induced denaturation of the lipoproteins in egg yolk, which prevented further fractionation of the yolk. Thermal pasteurization of egg yolk at 61.1 °C for 3.5 min as well as high hydrostatic pressure (HHP) treatment (400 MPa for 5 min) did not change (p < 0.05) the composition of egg yolk or yolk fractions after their recovery by centrifugation. Expressed as dry matter, folate in pasteurized yolk was measured to be 599 µg/100 g, while its concentration reached 1969.7 µg/100 g for pasteurized granule and 1902.5 µg/100 g for HHP-treated granule. Folate was not detected in plasma, emphasizing the complete separation of yolk folate into granule. Further, we studied the effect of HHP on different dilutions of egg yolk, which were then fractionated. Egg yolk was diluted with water at different concentrations (0.1, 1.0, 10, 25, and 50%), HHP-treated at 400 MPa for 5 min, and centrifuged. Characterization of the compositions of the separated granule and plasma followed. Folate was stable under the HHP conditions used. However, HHP caused separation of folate from the yolk structure into water-soluble plasma. After HHP processing, the amount of folate detected in the plasma fraction was significantly (p < 0.05) higher (1434.9 µg/100 g) in the 25% diluted samples but was significantly (p < 0.05) lower in HHP-treated granule samples. Native sodium dodecyl sulfate-polyacrylamide gel electrophoresis results showed that phosvitin, α-livetin, and apovitellenin VIa were the proteins most resistant to HHP. This study confirms that dilution of egg yolk before HHP treatment can significantly (p < 0.05) change the composition of granule and plasma fractions after centrifugal fractionation of egg yolk.
[Mh] Termos MeSH primário: Gema de Ovo/química
Ácido Fólico/isolamento & purificação
Manipulação de Alimentos/métodos
[Mh] Termos MeSH secundário: Animais
Fracionamento Químico
Galinhas
Proteínas do Ovo/química
Proteínas do Ovo/isolamento & purificação
Eletroforese em Gel de Poliacrilamida
Ácido Fólico/química
Manipulação de Alimentos/instrumentação
Congelamento
Temperatura Alta
Pressão Hidrostática
Pasteurização
Fosvitina/química
Fosvitina/isolamento & purificação
[Pt] Tipo de publicação:EVALUATION STUDIES; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Egg Proteins); 9008-28-0 (livetin); 9008-96-2 (Phosvitin); 935E97BOY8 (Folic Acid)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170915
[Lr] Data última revisão:
170915
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170811
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jafc.7b02892


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[PMID]:28690180
[Au] Autor:Wang J; Wang J; Zhang Z; Zhang X; Ru S; Dong Y
[Ad] Endereço:Marine Life Science College, Ocean University of China, Qingdao 266003, China.
[Ti] Título:Development of an immunosensor for quantifying zebrafish vitellogenin based on the Octet system.
[So] Source:Anal Biochem;533:60-65, 2017 Sep 15.
[Is] ISSN:1096-0309
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Vitellogenin (Vtg) is a sensitive biomarker for environmental estrogens. In this study, an immunosensor for quantifying zebrafish Vtg was developed using the Octet system. First, Protein A sensors were immobilized with purified anti-lipovitellin (Lv) antibody that demonstrated specificity to Vtg. Then, antibody-coated biosensors were immersed into zebrafish Lv standards and diluted samples. The Octet system measured and recorded kinetic parameters between antigens and captured antibody within 5 min. Sample Vtg concentrations were automatically calculated by interpolating relative binding rates observed with each sample and the immobilized anti-Lv antibody into the developed standard curve. The sensor arrays exhibited a wide linear range from 78 to 5000 ng/mL, and the inter-assay coefficient of variation was 0.66-1.97%. Furthermore, the performance of the immunosensor in detecting Vtg was evaluated by quantifying Vtg induction in juvenile zebrafish exposed to 17ß-estradiol (E ). Compared with conventional immunoassay techniques, the Vtg immunosensor developed based on the Octet system was much simpler and less time-consuming, allowing rapid Vtg quantification within 15 min. Moreover, Protein A sensors could be reused many times to ensure that the assays have high reproducibility. Therefore, we suggest that immunosensors based on the Octet system are an easily operated detection method for ecotoxicological research.
[Mh] Termos MeSH primário: Anticorpos Anti-Idiotípicos/isolamento & purificação
Técnicas Biossensoriais
Vitelogeninas/isolamento & purificação
[Mh] Termos MeSH secundário: Animais
Anticorpos Anti-Idiotípicos/imunologia
Proteínas do Ovo/imunologia
Estradiol/farmacologia
Proteína Estafilocócica A/química
Vitelogeninas/imunologia
Peixe-Zebra/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies, Anti-Idiotypic); 0 (Egg Proteins); 0 (Staphylococcal Protein A); 0 (Vitellogenins); 4TI98Z838E (Estradiol); 9088-43-1 (lipovitellin)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170804
[Lr] Data última revisão:
170804
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170711
[St] Status:MEDLINE


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[PMID]:28635261
[Au] Autor:Akyüz E; Baskan KS; Tütem E; Apak R
[Ad] Endereço:Department of Chemistry, Faculty of Engineering, Istanbul University , 34320 Istanbul, Turkey.
[Ti] Título:Novel Protein-Based Solid-Biosensor for Determining Pro-oxidant Activity of Phenolic Compounds.
[So] Source:J Agric Food Chem;65(28):5821-5830, 2017 Jul 19.
[Is] ISSN:1520-5118
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:To develop a protein-based biosensor measuring the pro-oxidant activities of phenolic compounds, egg white proteins were precipitated with calcium chloride to obtain an insoluble calcium proteinate complex. This biosensor was used for the determination of Cu(II)-induced pro-oxidant activity of antioxidants such as gallic acid, catechin, epicatechin, quercetin, chlorogenic acid and myricetin, and ascorbic acid. This assay involved the reduction of Cu(II) ions to Cu(I) by antioxidant compounds (simultaneously giving rise to reactive oxygen species) and binding of the formed Cu(I) to the solid biosensor. The protein-bound Cu(I), an indicator of pro-oxidant activity of antioxidants on proteins, was colorimetrically determined at 450 nm with neocuproine (Nc). The method was applied to synthetic mixtures and herbal (sage, green tea, mint, and marjoram) infusions, and its findings were compared to those of a modified carbonyl detection assay. This low-cost biosensor can be prepared in large quantities and used for a long time.
[Mh] Termos MeSH primário: Técnicas Biossensoriais/métodos
Proteínas do Ovo/química
Oxidantes/química
Fenóis/química
[Mh] Termos MeSH secundário: Animais
Antioxidantes/química
Galinhas
Cobre/química
Oxirredução
Chá/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antioxidants); 0 (Egg Proteins); 0 (Oxidants); 0 (Phenols); 0 (Tea); 789U1901C5 (Copper)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170728
[Lr] Data última revisão:
170728
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170622
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jafc.7b01649


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[PMID]:28622512
[Au] Autor:Raj I; Sadat Al Hosseini H; Dioguardi E; Nishimura K; Han L; Villa A; de Sanctis D; Jovine L
[Ad] Endereço:Department of Biosciences and Nutrition and Center for Innovative Medicine, Karolinska Institutet, Huddinge, SE-141 83, Sweden.
[Ti] Título:Structural Basis of Egg Coat-Sperm Recognition at Fertilization.
[So] Source:Cell;169(7):1315-1326.e17, 2017 Jun 15.
[Is] ISSN:1097-4172
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Recognition between sperm and the egg surface marks the beginning of life in all sexually reproducing organisms. This fundamental biological event depends on the species-specific interaction between rapidly evolving counterpart molecules on the gametes. We report biochemical, crystallographic, and mutational studies of domain repeats 1-3 of invertebrate egg coat protein VERL and their interaction with cognate sperm protein lysin. VERL repeats fold like the functionally essential N-terminal repeat of mammalian sperm receptor ZP2, whose structure is also described here. Whereas sequence-divergent repeat 1 does not bind lysin, repeat 3 binds it non-species specifically via a high-affinity, largely hydrophobic interface. Due to its intermediate binding affinity, repeat 2 selectively interacts with lysin from the same species. Exposure of a highly positively charged surface of VERL-bound lysin suggests that complex formation both disrupts the organization of egg coat filaments and triggers their electrostatic repulsion, thereby opening a hole for sperm penetration and fusion.
[Mh] Termos MeSH primário: Fertilização
Invertebrados/fisiologia
Vertebrados/fisiologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Evolução Biológica
Proteínas do Ovo/química
Proteínas do Ovo/metabolismo
Seres Humanos
Invertebrados/química
Invertebrados/genética
Masculino
Modelos Moleculares
Mucoproteínas/química
Mucoproteínas/metabolismo
Óvulo/química
Óvulo/metabolismo
Alinhamento de Sequência
Especificidade da Espécie
Espermatozoides/química
Espermatozoides/metabolismo
Vertebrados/genética
Difração de Raios X
Glicoproteínas da Zona Pelúcida/química
Glicoproteínas da Zona Pelúcida/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Egg Proteins); 0 (Mucoproteins); 0 (Zona Pellucida Glycoproteins); 0 (lysin, gastropoda)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170617
[St] Status:MEDLINE


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[PMID]:28622504
[Au] Autor:Hwang JY; Chung JJ
[Ad] Endereço:Department of Cellular & Molecular Physiology, Yale School of Medicine, New Haven, CT 06510, USA.
[Ti] Título:Sex at Atomic Resolution.
[So] Source:Cell;169(7):1174-1176, 2017 06 15.
[Is] ISSN:1097-4172
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Interspecies fertilization is rare, partly due to species separation enforced at the molecular level. In this issue, Raj et al. now reveal the crystal structures of mollusk egg coat protein, VERL, complexed with cognate sperm protein lysin. Given that VERL is structurally similar to mammalian ZP2, the mechanism elucidating species-specific gamete recognition likely exists in mammals.
[Mh] Termos MeSH primário: Proteínas do Ovo/química
Receptores de Superfície Celular/química
[Mh] Termos MeSH secundário: Animais
Fertilização
Masculino
Moluscos
Espermatozoides
[Pt] Tipo de publicação:JOURNAL ARTICLE; COMMENT
[Nm] Nome de substância:
0 (Egg Proteins); 0 (Receptors, Cell Surface)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170809
[Lr] Data última revisão:
170809
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170617
[St] Status:MEDLINE



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