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[PMID]:29227096
[Au] Autor:Song B; Oehrle NW; Liu S; Krishnan HB
[Ad] Endereço:Key Laboratory of Soybean Biology at the Chinese Ministry of Education, Northeast Agricultural University , Harbin 150030, China.
[Ti] Título:Development and Characterization of a Soybean Experimental Line Lacking the α' Subunit of ß-Conglycinin and G1, G2, and G4 Glycinin.
[So] Source:J Agric Food Chem;66(2):432-439, 2018 Jan 17.
[Is] ISSN:1520-5118
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:A soybean experimental line (BSH-3) devoid of a subset of seed storage proteins was developed by crossing a mutant donor line "HS99B" with a Chinese cultivar "Dongnong47" (DN47). One-dimensional and high-resolution 2-D gel electrophoresis revealed the absence of G1 (A1 B , G2 (A B1 , and G4 (A A B glycinin and the α' subunit of ß-conglycinin in BSH-3 seeds. Despite the lack of these abundant seed proteins, BSH-3 seeds still accumulated 38% protein. BSH-3 seeds also accumulated high levels of free amino acids as compared with DN47 seeds, particularly arginine, and the amount of several essential amino acids were significantly elevated in BSH-3 seeds. Elevated accumulation of α and ß-subunit of ß-conglycinin, G5 glycinin, Kunitz trypsin inhibitor, and Bowman-Birk protease inhibitor indicates seed proteome rebalancing in BSH-3 seeds. Immunoblot analysis using sera from soybean allergic patients demonstrated the complete lack of a major allergen (α' subunit of ß-conglycinin) in BSH-3 seeds. However, elevated levels of other allergens were found in BSH-3 seeds due to proteome rebalancing. Transmission electron microscopy observation of mature seeds of BSH-3 revealed striking differences in the appearance of the protein storage vacuoles when compared with DN47.
[Mh] Termos MeSH primário: Antígenos de Plantas/análise
Globulinas/análise
Proteínas de Armazenamento de Sementes/análise
Proteínas de Soja/análise
Feijão de Soja/química
[Mh] Termos MeSH secundário: Cruzamento
Eletroforese em Gel Bidimensional
Sementes/química
Sementes/genética
Feijão de Soja/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antigens, Plant); 0 (Globulins); 0 (Seed Storage Proteins); 0 (Soybean Proteins); 0 (beta-conglycinin protein, Glycine max); 9007-93-6 (glycinin)
[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:171212
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jafc.7b05011


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[PMID]:27771868
[Au] Autor:Schmidt MA; Pendarvis K
[Ad] Endereço:School of Plant Sciences, BIO5 Institute, University of Arizona, Tucson, AZ, USA. monicaschmidt@email.arizona.edu.
[Ti] Título:Proteome rebalancing in transgenic Camelina occurs within the enlarged proteome induced by ß-carotene accumulation and storage protein suppression.
[So] Source:Transgenic Res;26(2):171-186, 2017 04.
[Is] ISSN:1573-9368
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Oilseed crops are global commodities for their oil and protein seed content. We have engineered the oilseed Camelina sativa to exhibit increased protein content with a slight decrease in oil content. The introduction of a phytoene synthase gene with an RNAi cassette directed to suppress the storage protein 2S albumin resulted in seeds with an 11-24 % elevation in overall protein. The phytoene synthase cassette alone produced enhanced ß-carotene content of an average 275 ± 6.10 µg/g dry seed and an overall altered seed composition of 11 % less protein and comparable nontransgenic amounts of both oil and carbohydrates. Stacking an RNAi to suppress the major 2S storage protein resulted in seeds that contain elevated protein and slight decrease in oil and carbohydrate amounts showing that Camelina rebalances its proteome within an enlarged protein content genotype. In both ß-carotene enhanced seeds with/without RNAi2S suppression, the seed size was noticeably enlarged compared to nontransgenic counterpart seeds. Metabolic analysis of maturing seeds indicate that the enhanced ß-carotene trait had the larger effect than the RNAi2S suppression on the seed metabolome. The use of a GRAS (generally regarded as safe) ß-carotene as a visual marker in a floral dip transformation system, such as Camelina, might eliminate the need for costly regulatory and controversial antibiotic resistance markers. ß-carotene enhanced RNAi2S suppressed Camelina seeds could be further developed as a rapid heterologous protein production platform in a nonfood crop leveraging its enlarged protein content and visual marker.
[Mh] Termos MeSH primário: Plantas Geneticamente Modificadas/genética
Proteoma/genética
Proteínas de Armazenamento de Sementes/genética
beta Caroteno/metabolismo
[Mh] Termos MeSH secundário: Brassicaceae/genética
Brassicaceae/crescimento & desenvolvimento
Ácidos Graxos/metabolismo
Genótipo
Óleos Vegetais/metabolismo
Plantas Geneticamente Modificadas/metabolismo
Proteínas de Armazenamento de Sementes/metabolismo
beta Caroteno/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Fatty Acids); 0 (Plant Oils); 0 (Proteome); 0 (Seed Storage Proteins); 01YAE03M7J (beta Carotene)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180117
[Lr] Data última revisão:
180117
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161025
[St] Status:MEDLINE
[do] DOI:10.1007/s11248-016-9992-y


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[PMID]:28867186
[Au] Autor:Ikaga R; Li D; Yamazaki T
[Ad] Endereço:Department of Nutritional Science, National Institute of Health and Nutrition, National Institutes of Biomedical Innovation, Health and Nutrition, 1-23-1 Toyama, Shinjuku-ku, Tokyo, 162-8636, Japan.
[Ti] Título:Dietary ß-conglycinin prevents acute ethanol-induced fatty liver in mice.
[So] Source:Biochem Biophys Res Commun;493(1):542-547, 2017 Nov 04.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Alcoholic fatty liver is the earliest stage of alcohol-induced liver disease leading to liver cirrhosis. ß-Conglycinin, one of the soy proteins, is known to prevent non-alcoholic fatty liver, hyperlipidemia and obesity. Therefore, we examined whether ß-conglycinin feeding has an effect on the prevention of acute ethanol-induced fatty liver in mice. Male C57BL/6J mice were fed with 20 energy% ß-conglycinin or casein for 4 weeks prior to ethanol administration and were then given ethanol or glucose, as a control, by gavage. Ethanol significantly increased liver triglyceride (TG) in mice fed casein due to the activation of peroxisome proliferator-activated receptor (PPAR) γ2, a nuclear transcription factor known for regulating lipid metabolism and de novo lipogenesis. The liver TG of ethanol-administered ß-conglycinin-fed mice was significantly lower than that in those fed casein, although ethanol increased the amount of liver TG in mice fed ß-conglycinin. The increased levels of PPARγ2 protein and its target gene CD36 in response to an ethanol were not observed in mice fed ß-conglycinin. Moreover, ß-conglycinin decreased the basal expression of de novo lipogenesis-related genes such as stearoyl-CoA desaturase-1, and therefore, the expressions of these genes were lower in the ethanol-administered ß-conglycinin-fed mice than in the casein-fed mice. In conclusion, ß-conglycinin supplementation appears to prevent the development of fatty liver in mice caused by ethanol consumption via the suppression of alcohol-induced activation of PPARγ2 and the downregulation of the basal expression of de novo lipogenesis.
[Mh] Termos MeSH primário: Antígenos de Plantas/administração & dosagem
Suplementos Nutricionais
Globulinas/administração & dosagem
Lipogênese/efeitos dos fármacos
Hepatopatias Alcoólicas/metabolismo
Hepatopatias Alcoólicas/prevenção & controle
PPAR gama/metabolismo
Proteínas de Armazenamento de Sementes/administração & dosagem
Proteínas de Soja/administração & dosagem
[Mh] Termos MeSH secundário: Animais
Relação Dose-Resposta a Droga
Etanol/envenenamento
Hepatopatias Alcoólicas/etiologia
Masculino
Camundongos
Camundongos Endogâmicos C57BL
Resultado do Tratamento
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antigens, Plant); 0 (Globulins); 0 (PPAR gamma); 0 (Seed Storage Proteins); 0 (Soybean Proteins); 0 (beta-conglycinin protein, Glycine max); 3K9958V90M (Ethanol)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171023
[Lr] Data última revisão:
171023
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170905
[St] Status:MEDLINE


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[PMID]:28800361
[Au] Autor:Zhao L; Zhao L; Zhang B; Robotham JM; Roux KH; Tang H
[Ad] Endereço:Institute of Health Sciences, Anhui University, Hefei, Anhui, PR China.
[Ti] Título:Identification of a common Ara h 3 epitope recognized by both the capture and the detection monoclonal antibodies in an ELISA detection kit.
[So] Source:PLoS One;12(8):e0182935, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Allergy to peanuts has become a common and severe problem, especially in westernized countries. In this study, we evaluated the target and epitope specificity of the capture and detection mouse monoclonal antibodies (mAbs) used in a commercial peanut allergen detection platform. We first identified the target of these antibodies as Ara h 3 and then used an overlapping peptide array of Ara h 3 to determine the antibody-binding epitopes. Further amino acids critical for the binding via alanine substitutions at individual amino acid residues within the epitope were mapped. Finally, inhibition ELISA and inhibition immunoblotting using a recombinant Ara h 3 protein were performed to confirm these results. Surprisingly, the capture and detection mAbs showed identical binding characteristics and were presumed to represent two isolates of the same clone, a notion supported by both isoelectric focusing electrophoresis and Liquid chromatography-mass spectrometry experiments. The simultaneous binding of a pair of identical mAbs to an individual allergen such as Ara h3 is attributed to the multivalency of the analyte and has implications for developing diagnostic assays for additional multimeric allergens.
[Mh] Termos MeSH primário: Anticorpos Monoclonais/química
Antígenos de Plantas/química
Arachis/química
Epitopos/análise
Hipersensibilidade a Amendoim/diagnóstico
Proteínas de Plantas/química
Proteínas de Armazenamento de Sementes/química
[Mh] Termos MeSH secundário: Alanina/química
Alanina/genética
Alanina/imunologia
Alérgenos/química
Alérgenos/imunologia
Sequência de Aminoácidos
Substituição de Aminoácidos
Animais
Anticorpos Monoclonais/biossíntese
Anticorpos Monoclonais/isolamento & purificação
Antígenos de Plantas/genética
Antígenos de Plantas/imunologia
Arachis/imunologia
Ensaio de Imunoadsorção Enzimática/normas
Mapeamento de Epitopos
Epitopos/química
Epitopos/imunologia
Expressão Gênica
Seres Humanos
Camundongos
Modelos Moleculares
Hipersensibilidade a Amendoim/imunologia
Proteínas de Plantas/genética
Proteínas de Plantas/imunologia
Análise Serial de Proteínas
Multimerização Proteica
Estrutura Secundária de Proteína
Kit de Reagentes para Diagnóstico
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/imunologia
Proteínas de Armazenamento de Sementes/genética
Proteínas de Armazenamento de Sementes/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Allergens); 0 (Antibodies, Monoclonal); 0 (Antigens, Plant); 0 (Epitopes); 0 (Plant Proteins); 0 (Reagent Kits, Diagnostic); 0 (Recombinant Proteins); 0 (Seed Storage Proteins); 0 (allergen Ara h3); OF5P57N2ZX (Alanine)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171004
[Lr] Data última revisão:
171004
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170812
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0182935


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[PMID]:28795235
[Au] Autor:Brzostowski LF; Pruski TI; Specht JE; Diers BW
[Ad] Endereço:Department of Crop Sciences, University of Illinois, 1101 W. Peabody Drive, Urbana, IL, 61801, USA.
[Ti] Título:Impact of seed protein alleles from three soybean sources on seed composition and agronomic traits.
[So] Source:Theor Appl Genet;130(11):2315-2326, 2017 Nov.
[Is] ISSN:1432-2242
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:KEY MESSAGE: Evaluation of seed protein alleles in soybean populations showed that an increase in protein concentration is generally associated with a decrease in oil concentration and yield. Soybean [Glycine max (L.) Merrill] meal is one of the most important plant-based protein sources in the world. Developing cultivars high in seed protein concentration and seed yield is a difficult task because the traits have an inverse relationship. Over two decades ago, a protein quantitative trait loci (QTL) was mapped on chromosome (chr) 20, and this QTL has been mapped to the same position in several studies and given the confirmed QTL designation cqSeed protein-003. In addition, the wp allele on chr 2, which confers pink flower color, has also been associated with increased protein concentration. The objective of our study was to evaluate the effect of cqSeed protein-003 and the wp locus on seed composition and agronomic traits in elite soybean backgrounds adapted to the Midwestern USA. Segregating populations of isogenic lines were developed to test the wp allele and the chr 20 high protein QTL alleles from Danbaekkong (PI619083) and Glycine soja PI468916 at cqSeed protein-003. An increase in protein concentration and decrease in yield were generally coupled with the high protein alleles at cqSeed protein-003 across populations, whereas the effects of wp on protein concentration and yield were variable. These results not only demonstrate the difficulty in developing cultivars with increased protein and yield but also provide information for breeding programs seeking to improve seed composition and agronomic traits simultaneously.
[Mh] Termos MeSH primário: Proteínas de Armazenamento de Sementes/genética
Sementes/química
Feijão de Soja/genética
[Mh] Termos MeSH secundário: Alelos
Cruzamentos Genéticos
Marcadores Genéticos
Melhoramento Vegetal
Locos de Características Quantitativas
Sementes/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Genetic Markers); 0 (Seed Storage Proteins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171018
[Lr] Data última revisão:
171018
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170811
[St] Status:MEDLINE
[do] DOI:10.1007/s00122-017-2961-x


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[PMID]:28632187
[Au] Autor:Hsiao YH; Hsia SY; Chan YC; Hsieh JF
[Ad] Endereço:Ph.D. Program in Nutrition & Food Science, Fu Jen Catholic University, Taipei 24205, Taiwan. ariel.66@yahoo.com.tw.
[Ti] Título:Complex Coacervation of Soy Proteins, Isoflavones and Chitosan.
[So] Source:Molecules;22(6), 2017 Jun 20.
[Is] ISSN:1420-3049
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:In this study, the chitosan-induced coacervation of soy protein-isoflavone complexes in soymilk was investigated. Most of the soymilk proteins, including ß-conglycinin (7S), glycinin (11S), and isoflavones, were found to coacervate into the soymilk pellet fraction (SPF) following the addition of 0.5% chitosan. The total protein in the soymilk supernatant fraction (SSF) decreased from 18.1 ± 0.3 mg/mL to 1.6 ± 0.1 mg/mL, and the pH values decreased slightly, from 6.6 ± 0.0 to 6.0 ± 0.0. The results of SDS-PAGE revealed that the 7S α', 7S α, 7S ß, 11S A3, and 11S acidic subunits, as well as the 11S basic proteins in the SSF, decreased to 0.7 ± 0.5%, 0.2 ± 0.1%, 0.1 ± 0.0%, 0.2 ± 0.2%, 0.2 ± 0.2% and 0.3 ± 0.2%, respectively. We also found that isoflavones in the SSF, including daidzein, glycitein, and genistein, decreased to 9.6 ± 2.3%, 5.7 ± 0.9% and 5.9 ± 1.5%, respectively. HPLC analysis indicated that isoflavones mixed with soy proteins formed soy protein-isoflavone complexes and were precipitated into the SPF by 0.5% chitosan.
[Mh] Termos MeSH primário: Quitosana/química
Proteínas de Soja/química
[Mh] Termos MeSH secundário: Antígenos de Plantas/química
Cromatografia Líquida de Alta Pressão
Análise de Alimentos
Globulinas/química
Isoflavonas/química
Avaliação Nutricional
Proteínas de Armazenamento de Sementes/química
Leite de Soja/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antigens, Plant); 0 (Globulins); 0 (Isoflavones); 0 (Seed Storage Proteins); 0 (Soybean Proteins); 0 (beta-conglycinin protein, Glycine max); 9012-76-4 (Chitosan); 92M5F28TVF (glycitein)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170630
[Lr] Data última revisão:
170630
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170621
[St] Status:MEDLINE


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[PMID]:28630013
[Au] Autor:Kunz D; Oliveira GB; Uchôa AF; Samuels RI; Macedo MLR; Silva CP
[Ad] Endereço:Departamento de Bioquímica, Centro de Ciências Biológicas, Universidade Federal de Santa Catarina, C.P. 476, 88040-900 Florianópolis, SC, Brazil.
[Ti] Título:Receptor mediated endocytosis of vicilin in Callosobruchus maculatus (Coleoptera: Chrysomelidae) larval midgut epithelial cells.
[So] Source:Comp Biochem Physiol B Biochem Mol Biol;210:39-47, 2017 Aug.
[Is] ISSN:1879-1107
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The transport of proteins across the intestinal epithelium of insects is still not well understood. There is evidence that vicilin, a major storage protein of cowpea seeds (Vigna unguiculata), is internalized in larvae of the seed-beetle Callosobruchus maculatus. It has been reported that this vicilin interacts with proteins present in the microvillar membranes of columnar cells along the digestive tract of the larvae. In the present work, we studied the cellular pathway involved in endocytosis of vicilin in larval C. maculatus by employing ex vivo experiments. In the ex vivo approach, we incubated FITC-labelled vicilin with isolated midgut wholemounts in the absence or in the presence of endocytosis inhibitors. The fate of labelled or non-labelled globulins was monitored by confocal microscopy and fluorescence measurement. Our results suggest that the internalization of vicilins is due to receptor-mediated endocytosis. Here we report the identity of a microvillar vicilin-binding protein that was purified using affinity chromatography on a vicilin-sepharose column. The putative vicilin receptor showed high homology to proteins with the CRAL-TRIO domain, specifically the Sec14 superfamily member α-tocopherol transfer protein. The precise mechanism involved in vicilin internalization was defined through the use of specific inhibitors of the endocytosis pathway. The inhibitors filipin III and nystatin significantly inhibited the endocytosis of vicilin, while chlorpromazine and phenylarsine oxide had a much lower effect on endocytosis, suggesting that the endocytic pathway is predominantly mediated by caveolin.
[Mh] Termos MeSH primário: Proteínas de Transporte/metabolismo
Coleópteros/metabolismo
Células Epiteliais/metabolismo
Proteínas de Insetos/metabolismo
Larva/metabolismo
Proteínas de Armazenamento de Sementes/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Arsenicais/farmacologia
Transporte Biológico
Proteínas de Transporte/genética
Clorpromazina/farmacologia
Coleópteros/efeitos dos fármacos
Coleópteros/genética
Sistema Digestório/efeitos dos fármacos
Sistema Digestório/metabolismo
Sistema Digestório/ultraestrutura
Endocitose/efeitos dos fármacos
Endocitose/genética
Células Epiteliais/efeitos dos fármacos
Células Epiteliais/ultraestrutura
Filipina/farmacologia
Fluoresceína-5-Isotiocianato/química
Corantes Fluorescentes/química
Expressão Gênica
Proteínas de Insetos/genética
Larva/efeitos dos fármacos
Larva/genética
Nistatina/farmacologia
Proteínas de Armazenamento de Sementes/genética
Alinhamento de Sequência
Homologia de Sequência de Aminoácidos
Coloração e Rotulagem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Arsenicals); 0 (Carrier Proteins); 0 (Fluorescent Dyes); 0 (Insect Proteins); 0 (Seed Storage Proteins); 0 (alpha-tocopherol transfer protein); 0HUR2WY345 (oxophenylarsine); 1400-61-9 (Nystatin); 87Z59R7D14 (Filipin); 9067-60-1 (vicilin protein, plant); I223NX31W9 (Fluorescein-5-isothiocyanate); U42B7VYA4P (Chlorpromazine)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170621
[St] Status:MEDLINE


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[PMID]:28375469
[Au] Autor:Guénin S; Hardouin J; Paynel F; Müller K; Mongelard G; Driouich A; Lerouge P; Kermode AR; Lehner A; Mollet JC; Pelloux J; Gutierrez L; Mareck A
[Ad] Endereço:BIOPI Biologie des Plantes et Innovation EA3900, Université de Picardie Jules Verne, 33 Rue Saint Leu, 80039 Amiens Cedex, France.
[Ti] Título:AtPME3, a ubiquitous cell wall pectin methylesterase of Arabidopsis thaliana, alters the metabolism of cruciferin seed storage proteins during post-germinative growth of seedlings.
[So] Source:J Exp Bot;68(5):1083-1095, 2017 Feb 01.
[Is] ISSN:1460-2431
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:AtPME3 (At3g14310) is a ubiquitous cell wall pectin methylesterase. Atpme3-1 loss-of-function mutants exhibited distinct phenotypes from the wild type (WT), and were characterized by earlier germination and reduction of root hair production. These phenotypical traits were correlated with the accumulation of a 21.5-kDa protein in the different organs of 4-day-old Atpme3-1 seedlings grown in the dark, as well as in 6-week-old mutant plants. Microarray analysis showed significant down-regulation of the genes encoding several pectin-degrading enzymes and enzymes involved in lipid and protein metabolism in the hypocotyl of 4-day-old dark grown mutant seedlings. Accordingly, there was a decrease in proteolytic activity of the mutant as compared with the WT. Among the genes specifying seed storage proteins, two encoding CRUCIFERINS were up-regulated. Additional analysis by RT-qPCR showed an overexpression of four CRUCIFERIN genes in the mutant Atpme3-1, in which precursors of the α- and ß-subunits of CRUCIFERIN accumulated. Together, these results provide evidence for a link between AtPME3, present in the cell wall, and CRUCIFERIN metabolism that occurs in vacuoles.
[Mh] Termos MeSH primário: Proteínas de Arabidopsis/fisiologia
Arabidopsis/metabolismo
Hidrolases de Éster Carboxílico/fisiologia
Proteínas de Armazenamento de Sementes/metabolismo
Plântulas/crescimento & desenvolvimento
[Mh] Termos MeSH secundário: Arabidopsis/enzimologia
Arabidopsis/fisiologia
Parede Celular/enzimologia
Genes de Plantas/fisiologia
Germinação
Análise de Sequência com Séries de Oligonucleotídeos
Plântulas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Arabidopsis Proteins); 0 (Seed Storage Proteins); EC 3.1.1.- (Carboxylic Ester Hydrolases); EC 3.1.1.- (pectin methylesterase 3, Arabidopsis)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171113
[Lr] Data última revisão:
171113
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170405
[St] Status:MEDLINE
[do] DOI:10.1093/jxb/erx023


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[PMID]:28300503
[Au] Autor:Sirison J; Matsumiya K; Samoto M; Hidaka H; Kouno M; Matsumura Y
[Ad] Endereço:c Faculty of Agro-Industry , King Mongkut's Institute of Technology Ladkrabang , Bangkok , Thailand.
[Ti] Título:Solubility of soy lipophilic proteins: comparison with other soy protein fractions.
[So] Source:Biosci Biotechnol Biochem;81(4):790-802, 2017 Apr.
[Is] ISSN:1347-6947
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Solubility of soy lipophilic proteins (LP) was studied as compared with that of other soy protein fractions. LP, ß-conglycinin, glycinin, and soy protein isolate (N-SPI) were prepared under the condition to avoid heat denaturation. Solubility of LP was lower than that of other soy protein fractions under all the tested conditions varying in pH values and ionic strength. The solubility of LP was increased constantly by elevating temperature until 90 °C, whereas that of ß-conglycinin and glycinin dropped at high temperature. Temperature-dependent change in solubility of N-SPI might reflect the balance among that of glycinin, ß-conglycinin and LP. Based on the results of SDS-PAGE, determination of phospholipid content and Fourier Transform Infrared spectroscopy, we discussed the solubilization behavior of LP relating to its origin and composition.
[Mh] Termos MeSH primário: Antígenos de Plantas/química
Globulinas/química
Proteínas de Armazenamento de Sementes/química
Proteínas de Soja/química
[Mh] Termos MeSH secundário: Temperatura Alta
Desnaturação Proteica
Solubilidade
Espectroscopia de Infravermelho com Transformada de Fourier
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antigens, Plant); 0 (Globulins); 0 (Seed Storage Proteins); 0 (Soybean Proteins); 0 (beta-conglycinin protein, Glycine max); 9007-93-6 (glycinin)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170321
[Lr] Data última revisão:
170321
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170317
[St] Status:MEDLINE
[do] DOI:10.1080/09168451.2017.1282808


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[PMID]:28112517
[Au] Autor:Korte R; Happe J; Brümmer I; Brockmeyer J
[Ad] Endereço:Institute of Food Chemistry, Westfälische Wilhelms-Universität Münster , Corrensstraße 45, 48149 Münster, Germany.
[Ti] Título:Structural Characterization of the Allergenic 2S Albumin Cor a 14: Comparing Proteoform Patterns across Hazelnut Cultivars.
[So] Source:J Proteome Res;16(2):988-998, 2017 Feb 03.
[Is] ISSN:1535-3907
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The hazelnut allergen Cor a 14 belongs to the 2S albumins, a family of heterodimeric seed storage proteins exhibiting a high degree of structural diversity. Given its relevance as an allergen and the potential to elicit severe reactions, elucidation of the sequence heterogeneity of naturally occurring Cor a 14 is essential for the development of reliable diagnostics and risk evaluation. We therefore performed a comprehensive survey on the proteoforms of Cor a 14 and determined their quantitative distribution in three different hazelnut cultivars by a combinatory HPLC-HRMS approach including bottom-up and intact mass analysis. Compared with the Cor a 14 prototype sequence, we identified three sequence polymorphisms, two of the small and one of the large subunit, and elucidated their specific pairing on the protein level. Furthermore, we located a pronounced microheterogeneity on the protein termini and, for the first time, provide data on varying proteoform patterns between different cultivars of an allergenic seed. Together, these data present the basis for a more detailed investigation on the allergenicity of Cor a 14 in different cultivars and constitute, to be best of our knowledge, the largest set of proteoforms so far reported for a 2S albumin.
[Mh] Termos MeSH primário: Alérgenos/química
Antígenos de Plantas/química
Polimorfismo de Nucleotídeo Único
Subunidades Proteicas/química
Proteínas de Armazenamento de Sementes/química
[Mh] Termos MeSH secundário: Alérgenos/genética
Alérgenos/isolamento & purificação
Sequência de Aminoácidos
Antígenos de Plantas/genética
Antígenos de Plantas/isolamento & purificação
Cromatografia Líquida de Alta Pressão
Corylus/química
Expressão Gênica
Seres Humanos
Espectrometria de Massas
Isoformas de Proteínas/química
Isoformas de Proteínas/genética
Isoformas de Proteínas/isolamento & purificação
Subunidades Proteicas/genética
Subunidades Proteicas/isolamento & purificação
Proteínas de Armazenamento de Sementes/genética
Proteínas de Armazenamento de Sementes/isolamento & purificação
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Allergens); 0 (Antigens, Plant); 0 (Cor a 14 allergen, hazelnut); 0 (Protein Isoforms); 0 (Protein Subunits); 0 (Seed Storage Proteins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171016
[Lr] Data última revisão:
171016
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170124
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jproteome.6b00924



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