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A brief report on some health aspects of rats fed with crescent levels of recombinant chagasin, a potential plant defense protein Anais da ABC (AABC)
Oliveira Neto,Osmundo B.; Farias,Davi F.; Vasconcelos,Ilka M.; Paes,Norma S.; Monteiro,Ana C. S.; Silva,Maria C. M. da; Guimarães,Luciane M.; Carvalho,Ana F.U.; Grossi-de-Sá,Maria F..
Chagasin may be considered a potential plant-incorporated protectant (PIP) protein due to its deleterious effects on insect pests. However, extensive safety studies with PIP's are necessary before introducing them into the target plant. Thus, a short-term feeding trial in rats with high doses of r-chagasin was conducted to provide evidences about its safety. Three test diets containing casein + r-chagasin (0.25, 0.5 and 1% of total protein) were offered to rats (10 days). The test diets did not show adverse effects upon the development, organ weight, hematological parameters and serum protein profiles of rats, providing preliminary information on the safety of r-chagasin.
Tipo: Info:eu-repo/semantics/article Palavras-chave: Chagasin; Recombinant protein; Hazard potential; Short-term rat feeding trial.
Ano: 2012 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37652012000100019
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Applications of recombinant Pichia pastoris in the healthcare industry BJM
Weinacker,Daniel; Rabert,Claudia; Zepeda,Andrea B.; Figueroa,Carolina A.; Pessoa,Adalberto; Farías,Jorge G..
Since the 1970s, the establishment and development of the biotech industry has improved exponentially, allowing the commercial production of biopharmaceutical proteins. Nowadays, new recombinant protein production is considered a multibillion-dollar market, in which about 25% of commercial pharmaceuticals are biopharmaceuticals. But to achieve a competitive production process is not an easy task. Any production process has to be highly productive, efficient and economic. Despite that the perfect host is still not discovered, several research groups have chosen Pichia pastoris as expression system for the production of their protein because of its many features. The attempt of this review is to embrace several research lines that have adopted Pichia...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Yeast; Heterologous expression system; Recombinant protein; Production; Scale up.
Ano: 2013 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822013000400004
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Assessment of the acid phosphatase CP01850 from Corynebacterium pseudotuberculosis in DNA and subunit vaccine formulations against caseous lymphadenitis Arq. Bras. Med. Vet. Zootec.
Rezende,A.F.S.; Brum,A.A.; Bezerra,F.S.B.; Braite,D.C.; Sá,G.L.; Thurow,H.S.; Seixas,F.K.; Azevedo,V.A.C.; Portela,R.W.; Borsuk,S..
ABSTRACT The target cp1002_RS01850 from Corynebacterium pseudotuberculosis was used to construct a DNA and recombinant subunit vaccine against caseous lymphadenitis. Recombinant protein rCP01850 was expressed in Escherichia coli using pAE vector, and DNA vaccine was engineered with pTARGET vector. BALB/c mice were divided in five groups containing eight animals each, inoculated with: pTARGET/cp01850 as DNA vaccine (G1); rCP01850 plus Al (OH)3 as recombinant subunit vaccine (G2); pTARGET/cp01850 and a boost with rCP01850 plus Al (OH)3 (G3); pTARGET (G4); or Al (OH)3 (G5). Mice were inoculated and blood samples were collected on days 0, 21, and 42 for the analysis of total IgG, IgG1 and IgG2a by ELISA. In each group, five animals were challenged with Mic-6...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Cp1002_RS01850 gene; Immunization; Recombinant protein; Aluminum hydroxide; Heterologous prime-boost strategy.
Ano: 2020 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0102-09352020000100199
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Cloning, expression and characterization of alcohol dehydrogenases in the silkworm Bombyx mori Genet. Mol. Biol.
Wang,Nan; Shi,Haifeng; Yao,Qin; Zhou,Yang; Kang,Lequn; Chen,Huiqin; Chen,Keping.
Alcohol dehydrogenases (ADH) are a class of enzymes that catalyze the reversible oxidation of alcohols to corresponding aldehydes or ketones, by using either nicotinamide adenine dinucleotide (NAD) or nicotinamide adenine dinucleotide phosphate (NADP), as coenzymes. In this study, a short-chain ADH gene was identified in Bombyx mori by 5'-RACE PCR. This is the first time the coding region of BmADH has been cloned, expressed, purified and then characterized. The cDNA fragment encoding the BmADH protein was amplified from a pool of silkworm cDNAs by PCR, and then cloned into E. coli expression vector pET-30a(+). The recombinant His-tagged BmADH protein was expressed in E. coli BL21 (DE3), and then purified by metal chelating affinity chromatography. The...
Tipo: Info:eu-repo/semantics/article Palavras-chave: 5'-RACE PCRADH; Enzymatic activity; Recombinant protein.
Ano: 2011 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1415-47572011000200013
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Effects of A Recombinant Sarcocystis muris Microneme Protein on Splenocytes of The Natural Intermediate Host OAK
Klein, Harald; Zyto, Nadja; Loeschner, Bettina; Bornhak, Monika; Montag, Thomas.
Palavras-chave: Sarcocystis muris; Micronemes; Recombinant protein; Lectin; Immunosuppression.
Ano: 1998 URL: http://ir.obihiro.ac.jp/dspace/handle/10322/279
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Efficient expression and characterization of a cold-active endo-1, 4-β-glucanase from Citrobacter farmeri by co-expression of Myxococcus xanthus protein S Electron. J. Biotechnol.
Bai,Xi; Yuan,Xianjun; Wen,Aiyou; Li,Junfeng; Bai,Yunfeng; Shao,Tao.
Background: Cold-active endo-1, 4-β-glucanase (EglC) can decrease energy costs and prevent product denaturation in biotechnological processes. However, the nature EglC from C. farmeri A1 showed very low activity (800 U/L). In an attempt to increase its expression level, C. farmeri EglC was expressed in Escherichia coli as an N-terminal fusion to protein S (ProS) from Myxococcus xanthus. Results: A novel expression vector, pET(ProS-EglC), was successfully constructed for the expression of C. farmeri EglC in E. coli. SDS-PAGE showed that the recombinant protein (ProS-EglC) was approximately 60 kDa. The activity of ProS-EglC was 12,400 U/L, which was considerably higher than that of the nature EglC (800 U/L). ProS-EglC was active at pH 6.5-pH 8.0,...
Tipo: Journal article Palavras-chave: Cellulose degradation; Cellulose; Cold-active enzyme; Endoglucanases; Enzymatic properties; Escherichia coli; Expression; Novel expression vector; N-terminal fusion; Protein S-tag; Recombinant protein.
Ano: 2016 URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582016000600012
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Expression and biological activity of two recombinant polypeptides related to subunit 1 of the interferon-a receptor BJMBR
Yoon,S.; Hirata,R.D.C.; Nguyen,N.Y.; Curi,R.; Russo,M.; Hirata,M.H..
Abnormal production of interferon alpha (IFN-a) has been found in certain autoimmune diseases and can be also observed after prolonged therapy with IFN-a. IFN-a can contribute to the pathogenesis of allograft rejection in bone marrow transplants. Therefore, the development of IFN-a inhibitors as a soluble receptor protein may be valuable for the therapeutic control of these diseases. We have expressed two polypeptides encoding amino acids 93-260 (P1) and 261-410 (P2) of the extracellular domain of subunit 1 of the interferon-a receptor (IFNAR 1-EC) in E. coli. The activities of the recombinant polypeptides and of their respective antibodies were evaluated using antiproliferative and antiviral assays. Expression of P1 and P2 polypeptides was achieved by...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Interferon alpha; Interferon-a receptor; Inhibitor of interferon-a; Autoimmune diseases; Graft-versus-host disease; Recombinant protein.
Ano: 2000 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2000000700007
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Expression of Grapevine leafroll-associated virus 3 coat protein gene in Escherichia coli and production of polyclonal antibodies Trop. Plant Pathol.
Fajardo,Thor V.M.; Barros,Danielle R.; Nickel,Osmar; Kuhn,Gilmar B.; Zerbini,F. Murilo.
Grapevine leafroll-associated virus 3 (GLRaV-3), the main viral species of the grapevine leafroll complex, causes yield and quality reduction in grapes (Vitis spp.). The coat protein gene was RT-PCR-amplified from total RNA extracted from infected grapevine leaves and the amplified fragment was cloned and completely sequenced. The fragment was subsequently subcloned into the pRSET-C expression vector. The recombinant plasmid was used to transform Escherichia coli BL21:DE3 and express the capsid protein. The coat protein, fused to a 6 His-tag, was purified by affinity chromatography using an Ni-NTA resin. The identity of the purified protein was confirmed by SDS-PAGE and Western blot. The in vitro-expressed protein was quantified and used for rabbit...
Tipo: Info:eu-repo/semantics/other Palavras-chave: Grapevine; GLRaV-3; Recombinant protein; Serology; Antibodies.
Ano: 2007 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-41582007000600007
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Fermentation optimization of maltose-binding protein fused to neutrophil-activating protein from Escherichia coli TB1 Electron. J. Biotechnol.
Lu,Jike; Song,Qi; Ji,Zhenyu; Liu,Xin; Wang,Ting; Kang,Qiaozhen.
Background The fermentation conditions of recombinant maltose-binding protein fused to neutrophil-activating protein (rMBP-NAP) of Helicobacter pylori were optimized from Escherichia coli TB1 with varying medium, inoculum age and size, time, inducer, pH and temperature in batch fermentation. Results It was revealed that the optimal conditions for the production of rMBP-NAP in shake flask were as follows: M9 medium (with 3% yeast extract powder added), inoculum age of 19 h, inoculum size of 6%, initial pH of 6.6, temperature of 37°C, and 0.7 mmoL/L IPTG inducted 21 h in a 50 mL/250 mL shake flask. The recombinant protein yield was increased from 59 to 592 mg/L after optimization. Fermentation process conducted in a 10 L fermenter with similar conditions...
Tipo: Journal article Palavras-chave: Escherichia coli; Fermentation; Optimization; Recombinant protein.
Ano: 2015 URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582015000400004
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Growth hormone-insuline-like growth factor-I system in pejerrey Odontesthes bonariensis (Atheriniformes) R. Bras. Zootec.
Arranz,S.E.; Sciara,A. A.; Botta,P.; Cerutti,P.; Tobin,M.; Somoza,G.M..
Using biotechnology to increase the growth rates of fish is likely to reduce production costs per unit of food. Among vertebrates, fish appear to occupy a unique position, when growth patterns are considered. With few exceptions, fish species tend to grow indeterminately, implying that size is never fixed. Both hyperplasia and hypertrophy contribute to post-larval muscle growth in fish. Growth hormone (GH) - Insulin-like Growth Factor I (IGF-I) is the most important growth axis in fish. Our experimental model, the pejerrey, Odontesthes bonariensis (Ateriniformes) is a South American inland water fish considered to be a promising species for intensive aquaculture. However, one major drawback to achieve this goal is its slow growth in captivity. In order to...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Growth; Growth hormone; Muscle hypertrophy; Oral administration; Recombinant protein.
Ano: 2008 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1516-35982008001300001
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High expression of human carboxypeptidase M in Pichia pastoris: Purification and partial characterization BJMBR
Craveiro,R.B.; Ramalho,J.D.; Chagas,J.R.; Wang,P.H.M.; Casarini,D.E.; Pesquero,J.L.; Araújo,R.C.; Pesquero,J.B..
Carboxypeptidase M (CPM) is an extracellular glycosylphosphatidyl-inositol-anchored membrane glycoprotein, which removes the C-terminal basic residues, lysine and arginine, from peptides and proteins at neutral pH. CPM plays an important role in the control of peptide hormones and growth factor activity on the cell surface. The present study was carried out to clone and express human CPM in the yeast Pichia pastoris in order to evaluate the importance of this enzyme in physiological and pathological processes. The cDNA for the enzyme was amplified from total placental RNA by RT-PCR and cloned in the vector pPIC9, which uses the methanol oxidase promoter and drives the expression of high levels of heterologous proteins in P. pastoris. The cpm gene, after...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Kinins; Human carboxypeptidase M; Recombinant protein; Pichia pastoris.
Ano: 2006 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2006000200007
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High-level soluble expression of the functional peptide derived from the C-terminal domain of the sea cucumber lysozyme and analysis of its antimicrobial activity Electron. J. Biotechnol.
Cong,Lina; Liang,Wenjing; Wu,Yao; Li,Cheng; Chang,Yihai; Dong,Liang; Song,Wanlin; Ma,Jun.
Background The sea cucumber lysozyme belongs to the family of invertebrate lysozymes and is thought to be a key defense factor in protecting aquaculture animals against bacterial infection. Recently, evidence was found that the sea cucumber lysozyme exerts broad spectrum antimicrobial action in vitro against Gram-negative and Gram-positive bacteria, and it also has more potent antimicrobial activity independent of its enzymatic activity. To explore the antimicrobial role of this non-enzymatic lysozyme and model its structure to novel antimicrobial peptides, the peptide from the C-terminal amino acid residues 70-146 of the sea cucumber lysozyme in Stichopus japonicus (SjLys-C) was heterologously expressed in Escherichia coli Rosetta(DE3)pLysS. Results The...
Tipo: Journal article Palavras-chave: Affinity purification; Lysozyme peptide; Molecular modeling; Recombinant protein.
Ano: 2014 URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582014000600005
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Influence of culture medium on the production of eif antigen from Leishmania chagasi in recombinant Escherichia coli BJM
Vaz,Michelle Rossana Ferreira; França,Ricardo Luiz Soares de; Andrade,Sirtys Santos Lessa de; Sousa Junior,Francisco Canindé de; Santos,Everaldo Silvino dos; Martins,Daniella Regina Arantes; Macedo,Gorete Ribeiro de.
With the advent of recombinant DNA technology, recombinant protein expression has become an important tool in the study of the structure, function and identification of new proteins, especially those with therapeutic functions. Escherichia coli has been the predominant prokaryote used in genetic engineering studies due to the abundance of information about its metabolism. Despite significant advances in molecular biology and immunology of infections, there are as yet no prophylactic drugs capable of preventing visceral leishmaniasis. It is therefore important to identify specific antigens in order to develop vaccines and diagnostic kits against this disease. The objective of this study was to evaluate the influence of culture medium on the production of...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Cultivation; Recombinant protein; Visceral leishmaniasis; Escherichia coli.
Ano: 2011 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822011000400021
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Molecular cloning and expression of a computationally predicted surface antigen of Mycoplasma gallisepticum Rev Salud Anim.
Agüero,José Antonio; Aguilar-Bultet,Lisandra; Rodríguez,Ariadna.
Mycoplasmas, the simplest self-replicating organisms known, are distinguished phenotypically from other bacteria by their minute size and total lack of cell wall. The poultry industry is affected by several species of mycoplasmas, but Mycoplasma gallisepticum (MG) is the most economically significant one. The attachment of mycoplasmas to host respiratory epithelial cells constitutes a critical step in the pathway leading to infection and disease and is achieved by lipoproteins localized on the bacterial surface. In a recent in silico study, it was predicted a set of MG putative surface proteins with potential antigenic properties that could be used as candidates for exploring new vaccines, and for diagnostic tests as well. One of those potential candidates...
Tipo: Journal article Palavras-chave: Mycoplasma gallisepticum; Surface protein; Recombinant protein; IMAC purification.
Ano: 2015 URL: http://scielo.sld.cu/scielo.php?script=sci_arttext&pid=S0253-570X2015000100004
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MOLECULAR CLONING AND EXPRESSION OF A FRAGMENT OF THE GENE CODIFYING FOR THE PROTEIN ERNS OF CLASSICAL SWINE FEVER VIRUS Rev Salud Anim.
Agüero,J.A; Sánchez,O; Barrera,Maritza; Toledo,J.R.
Classical swine fever virus (CSFV), belonging to the genus Pestivirus of the Flaviviridae family, is an enveloped positive stranded RNA virus highly contagious that can cause a fatal disease, characterized by fever, leukopenia and hemorrhage, with substantial economic losses. There is a great demand for a marker vaccine against CSFV. C, Erns, E1, and E2 are the structural proteins of the virus. E2 is the best candidate to be incorporated in vaccine, while Erns becomes an ideal candidate as an antigen in a differential diagnostic test. A synthetic fragment of the Erns gene (codifying for aa 109-160) was subcloned into pET28a vector. The cloning was screened by restriction analysis. The gene was expressed as a his-tag fusion protein in BL21 (DE3) E. coli...
Tipo: Journal article Palavras-chave: Erns; CSFV; Recombinant protein; IMAC.
Ano: 2008 URL: http://scielo.sld.cu/scielo.php?script=sci_arttext&pid=S0253-570X2008000200003
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Molecular cloning and expression of a putative crustacean hyperglycemic hormone of Litopenaeus vannamei in Pichia pastoris Electron. J. Biotechnol.
Sánchez-Castrejón,Edna; Ponce-Rivas,Elizabeth; Aguilar,Manuel B; Díaz,Fernando.
Crustacean hyperglycemic hormone (CHH) is the most abundant and best studied member of the CHH/MIH/GIH neuropeptide hormone family. CHH plays a major role in controlling glucose levels in the hemolymph, and it also has significance in regulating molting, reproduction, and osmoregulation. In contrast, molt-inhibiting hormone (MIH) is responsible for maintaining animals in an intermolt stage. In this study, Liv-MIH-1 cDNA, which encodes a mature neuropeptide from the eyestalk of white shrimp, Litopenaeus vannamei, was expressed in methylotrophic yeast (Pichia pastoris KM71) under the control of an alcohol oxidase promoter. Recombinant Liv-MIH-1 was secreted into the culture medium using the α-factor prepro-sequence without Glu-Ala repeats. The...
Tipo: Journal article Palavras-chave: CHH; Litopenaeus vannamei; Pichia pastoris; Recombinant protein.
Ano: 2008 URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582008000400009
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Molecular cloning and expression of key gene encoding hypothetical DNA polymerase from B. mori parvo-like virus Genet. Mol. Biol.
Zhang,Junhong; Li,Guohui; Chen,Huiqing; Li,Xiaogang; Lv,Meng; Chen,Keping; Yao,Qin.
BmPLV-Z is the abbreviation for Bombyx mori parvo-like virus (China isolate). This is a novel virus with two single-stranded linear DNA molecules, viz., VD1 (6543 bp) and VD2 (6022 bp), which are encapsidated respectively into separate virions. Analysis of the deduced amino acid sequence of VD1-ORF4 indicated the existence of a putative DNA-polymerase with exonuclease activity, possibly involved in the replication of BmPLV-Z. In the present study, a recombinant baculovirus was constructed to express the full length of the protein encoded by the VD1-ORF4 gene (3318 bp). In addition, a 2163-bp fragment amplified from the very same gene was cloned into prokaryotic expression vector pET-30a and expressed in E.coli Rosetta 2 (DE3) pLysS. The expressed fusion...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Bombyx mori parvo-like virus; DNA polymerase; Recombinant protein; Sf-9.
Ano: 2010 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1415-47572010000400021
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Molecular cloning and recombinant expression of the VP28 carboxyl-terminal hydrophilic region from a brazilian white spot syndrome virus isolate BABT
Braunig,Patricia; Rosa,Rafael Diego da; Seibert,Caroline Heidrich; Borsa,Mariana; Stoco,Patricia Hermes; Grisard,Edmundo Carlos; Pinto,Aguinaldo Roberto.
In the present study, a fragment of the VP28 coding sequence from a Brazilian WSSV isolate (BrVP28) was cloned, sequenced and expressed in E. coli BL21(DE3) pLysS strain in order to produce the VP28 carboxyl-terminal hydrophilic region. The expression resulted in a protein of about 21 kDa, which was purified under denaturing conditions, resulting in a final highly purified BrVP28 preparation. The recombinant protein obtained can be used in several biotechnology applications, such as the production of monoclonal antibodies which could be used in the development of diagnostic tools as well as in the studies on the characterization of white spot syndrome virus (WSSV) isolated in Brazil.
Tipo: Info:eu-repo/semantics/article Palavras-chave: WSSV; VP28; Recombinant protein; Penaeid shrimp.
Ano: 2011 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132011000200023
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Production of antibody fragment (Fab) throughout Escherichia coli fed-batch fermentation process: Changes in titre, location and form of product Electron. J. Biotechnol.
Jalalirad,Reza.
Background: Recombinant proteins, including antibodies and antibody fragments, often contain disulfide bond bridges that are necessary for their folding, stability and function. Production of disulfide-bond-containing proteins in the periplasm of Escherichia coli has been very useful, due to unique characteristics of the periplasm, for obtaining fully active and correctly folded products and for alleviating downstream processing. Results: In this study, fed-batch cultivation of Escherichia coli (E. coli) for production of Fab D1.3, which is an anti-hen egg white lysozyme (HEWL) antibody fragment was carried out at 37ºC, and the bacterial cells were induced by adding 0.1 mM IPTG to the culture medium. Fermentor was sampled over the course of fermentation;...
Tipo: Journal article Palavras-chave: Antibody fragment; Cell disruption; Escherichia coli; Fed-batch fermentation; Periplasmic expression; Recombinant protein.
Ano: 2013 URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582013000300009
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Production of polyclonal antisera using recombinant coat proteins of Grapevine leafroll-associated virus 2 and Grapevine virus B PAB
Radaelli,Paula; Fajardo,Thor Vinícius Martins; Nickel,Osmar; Eiras,Marcelo; Pio-Ribeiro,Gilvan.
The objective of this work was to produce and characterize specific antisera against Brazilian isolates of Grapevine leafroll-associated virus 2 (GLRaV-2) and Grapevine virus B (GVB), developed from expressed coat proteins (CPs) in Escherichia coli, and to test their possible use for the detection of these two viruses in diseased grapevines. The coat protein (CP) genes were RT-PCR-amplified, cloned and sequenced. The CP genes were subsequently subcloned, and the recombinant plasmids were used to transform E. coli cells and express the coat proteins. The recombinant coat proteins were purified, and their identities were confirmed by SDS-PAGE and Western blot and used for rabbit immunizations. Antisera raised against these proteins were able to recognize the...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Vitis; GLRaV-2; GVB; Indirect ELISA; Recombinant protein; Western blot.
Ano: 2008 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-204X2008001000020
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