|
|
|
| Registros recuperados: 22 | |
|
|
| 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 |
| |
|
|
| 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 |
| |
|
|
| 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 |
| |
|
|
| 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 |
| |
|
| |
|
|
| 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 |
| |
|
| |
|
| |
|
|
| 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 |
| |
|
|
| 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 |
| |
|
|
| 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 |
| |
|
|
| 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 |
| |
|
|
| 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 |
| |
|
| |
|
|
| 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 |
| |
|
|
| 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 |
| |
|
|
| 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 |
| |
|
|
| 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 |
| |
|
| |
|
|
| 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 |
| |
| Registros recuperados: 22 | |
|
|
|
