Base de dados : LILACS
Pesquisa : D08.811.277.450.207 [Categoria DeCS]
Referências encontradas : 29 [refinar]
Mostrando: 1 .. 10   no formato [Detalhado]

página 1 de 3 ir para página          

  1 / 29 LILACS  
              next record last record
seleciona
para imprimir
Fotocópia
Texto completo SciELO Brasil
Texto completo
Id: biblio-1132157
Autor: Okay, Sezer; Alshehri, Wafa Abduallah.
Título: Overexpression of Chitinase A Gene from Serratia marcescens in Bacillus subtilis and Characterization of Enhanced Chitinolytic Activity
Fonte: Braz. arch. biol. technol;63:e20200061, 2020. graf.
Idioma: en.
Resumo: Abstract Chitinase enzymes possess various usages in agriculture, biotechnology and medicine due to their chitin degrading property. Thus, efficient production of chitinase enzymes with desired properties has importance for its use. In this study, chitinase A (chiA) gene from Serratia marcescens Bn10 was cloned and heterologously overexpressed using pHT43 vector in Bacillus subtilis 168. The recombinant chitinase was characterized in terms of temperature, pH, and various effectors. The extracellular chitinase activity in recombinant B. subtilis was found 2.15-fold higher than the parental strain after 2 h of IPTG induction. Optimum temperature and pH for the extracellular chitinase activity in the recombinant B. subtilis were determined as 60 oC and pH 9.0, respectively. NaCl, Ca2+, Mn2+, Cu2+, Zn2+, sodium dodecyl sulfate (SDS), Tween-20, and ethanol increased the chitinase activity whereas Mg2+ caused an inhibition. The most notable increment on the chitinase activity was provided by Zn2+ (3.2 folds) and then by SDS (2.9 folds). The chitinase, overproduced by the recombinant B. subtilis 168 heterologously expressing chiA, was determined to have optimum activity at high temperature and alkaline conditions as well as various effectors increase its activity. The extracellular chitinase of recombinant B. subtilis might be a promising source for agricultural, biotechnological and medical applications.
Descritores: Serratia marcescens/enzimologia
Bacillus subtilis/enzimologia
Quitinases/genética
Concentração de Íons de Hidrogênio
-Temperatura
Expressão Gênica
Responsável: BR1.1 - BIREME


  2 / 29 LILACS  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
Id: biblio-1052045
Autor: Zhao, Xiaobo; Li, Chunjuan; Yan, Caixia; Wang, Juan; Yuan, Cuiling; Zhang, Hao; Shan, Shihua.
Título: Transcriptome and proteome analyses of resistant preharvest peanut seed coat in response to Aspergillus flavus infection
Fonte: Electron. j. biotechnol;39:82-90, may. 2019. graf, ilus.
Idioma: en.
Projeto: Taishan Scholar Project of Shandong Province, China; . Agro-industry Technology Research System of Shandong Province, China; . Fine Breeding Project of Shandong Province, China; . Agricultural Scientific and Technological Innovation Project of Shandong Academy of Agricultural Sciences, China.
Resumo: BACKGROUND: The infection of peanut (Arachis hypogaea L.) seed coat by the pathogenic fungus Aspergillus flavus has highly negative economic and health impacts. However, the molecular mechanism underlying such defense response remains poorly understood. This study aims to address this issue by profiling the transcriptomic and proteomic changes that occur during the infection of the resistant peanut cultivar J11 by A. flavus. RESULTS: Transcriptomic study led to the detection of 13,539 genes, among which 663 exhibited differential expression. Further functional analysis found the differentially expressed genes to encode a wide range of pathogenesis- and/or defense-related proteins such as transcription factors, pathogenesis-related proteins, and chitinases. Changes in the expression patterns of these genes might contribute to peanut resistance to A. flavus. On the other hand, the proteomic profiling showed that 314 of the 1382 detected protein candidates were aberrantly expressed as a result of A. flavus invasion. However, the correlation between the transcriptomic and proteomic data was poor. We further demonstrated by in vitro fungistasis tests that hevamine-A, which was enriched at both transcript and protein levels, could directly inhibit the growth of A. flavus. Conclusions: The results demonstrate the power of complementary transcriptomic and proteomic analyses in the study of pathogen defense and resistance in plants and the chitinase could play an important role in the defense response of peanut to A. flavus. The current study also constitutes the first step toward building an integrated omics data platform for the development of Aspergillus-resistant peanut cultivars
Descritores: Arachis/genética
Proteoma/análise
Transcriptoma
-Arachis/microbiologia
Aspergillus flavus/fisiologia
Sementes/genética
Expressão Gênica
Quitinases
Aflatoxinas
Resistência à Doença/genética
Reação em Cadeia da Polimerase em Tempo Real
RNA-Seq
Responsável: CL1.1 - Biblioteca Central


  3 / 29 LILACS  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo SciELO Brasil
Texto completo
Id: biblio-1042513
Autor: Soares, Alexandra Martins dos Santos; Wanderley, Lêdia Feitosa; Costa Junior, Livio Martins.
Título: The potential of plant and fungal proteins in the control of gastrointestinal nematodes from animals / Potencial de proteínas de plantas e fungos no controle de nematoides gastrintestinais de animais
Fonte: Rev. bras. parasitol. vet;28(3):339-345, July-Sept. 2019.
Idioma: en.
Resumo: Abstract Gastrointestinal nematode infection is an important cause of high economic losses in livestock production. Nematode control based on a synthetic chemical approach is considered unsustainable due to the increasing incidence of anthelmintic resistance. Control alternatives such as the use of natural products are therefore becoming relevant from an environmental and economic point of view. Proteins are macromolecules with various properties that can be obtained from a wide range of organisms, including plants and fungi. Proteins belonging to different classes have shown great potential for the control of nematodes. The action of proteins can occur at specific stages of the nematode life cycle, depending on the composition of the external layers of the nematode body and the active site of the protein. Advances in biotechnology have resulted in the emergence of numerous protein and peptide therapeutics; however, few have been discussed with a focus on the control of animal nematodes. Here, we discuss the use of exogenous proteins and peptides in the control of gastrointestinal.

Resumo A infecção por nematoides gastrintestinais é uma importante causa de grandes perdas econômicas na pecuária. O controle de nematoides com compostos químicos sintéticos é considerado insustentável devido ao aumento da resistência anti-helmíntica. Alternativas de controle, como o uso de produtos naturais, estão se tornando relevantes do ponto de vista ambiental e econômico. As proteínas são macromoléculas com várias propriedades que podem ser obtidas de uma ampla gama de organismos, incluindo plantas e fungos. Proteínas pertencentes a diferentes classes têm mostrado grande potencial para o controle de nematoides. A ação das proteínas pode ocorrer em estágios específicos do ciclo de vida do nematoide, dependendo da composição das camadas externas do parasito e do sítio ativo da proteína. Avanços na biotecnologia resultaram no surgimento de numerosas terapias de proteínas e peptídeos; no entanto, pouco foi discutido com foco no controle de nematoides parasitos de animais. Na presente revisão foi discutido o uso de proteínas exógenas e peptídeos no controle de nematoides gastrintestinais, os mecanismos sugeridos de ação, e os desafios e perspectivas para o uso dessas biomoléculas como uma classe de anti-helmínticos.
Descritores: Peptídeos/isolamento & purificação
Proteínas de Plantas/isolamento & purificação
Proteínas Fúngicas/isolamento & purificação
Gastroenteropatias/veterinária
Infecções por Nematoides/veterinária
Antinematódeos/isolamento & purificação
-Peptídeo Hidrolases/administração & dosagem
Peptídeo Hidrolases/isolamento & purificação
Peptídeos/administração & dosagem
Proteínas de Plantas/administração & dosagem
Biotecnologia
Proteínas Fúngicas/administração & dosagem
Quitinases/administração & dosagem
Quitinases/isolamento & purificação
Gastroenteropatias/parasitologia
Infecções por Nematoides/tratamento farmacológico
Antinematódeos/administração & dosagem
Limites: Animais
Tipo de Publ: Revisão
Responsável: BR1.1 - BIREME


  4 / 29 LILACS  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo SciELO Brasil
Texto completo
Id: biblio-828205
Autor: Aliabadi, Nasrin; Aminzadeh, Saeed; Karkhane, Ali Asghar; Haghbeen, Kamahldin.
Título: Thermostable chitinase from Cohnella sp. A01: isolation and product optimization
Fonte: Braz. j. microbiol;47(4):931-940, Oct.-Dec. 2016. tab, graf.
Idioma: en.
Projeto: International Foundation for Science; . Committee on Scientific and Technological Cooperation; . National Institute of Genetic Engineering and Biotechnology.
Resumo: Abstract Twelve bacterial strains isolated from shrimp farming ponds were screened for their growth activity on chitin as the sole carbon source. The highly chitinolytic bacterial strain was detected by qualitative cup plate assay and tentatively identified to be Cohnella sp. A01 based on 16S rDNA sequencing and by matching the key morphological, physiological, and biochemical characteristics. The cultivation of Cohnella sp. A01 in the suitable liquid medium resulted in the production of high levels of enzyme. The colloidal chitin, peptone, and K2HPO4 represented the best carbon, nitrogen, and phosphorus sources, respectively. Enzyme production by Cohnella sp. A01 was optimized by the Taguchi method. Our results demonstrated that inoculation amount and temperature of incubation were the most significant factors influencing chitinase production. From the tested values, the best pH/temperature was obtained at pH 5 and 70 °C, with Km and V max values of chitinase to be 5.6 mg/mL and 0.87 µmol/min, respectively. Ag+, Co2+, iodoacetamide, and iodoacetic acid inhibited the enzyme activity, whereas Mn2+, Cu2+, Tweens (20 and 80), Triton X-100, and EDTA increased the same. In addition, the study of the morphological alteration of chitin treated by enzyme by SEM revealed cracks and pores on the chitin surface, indicating a potential application of this enzyme in several industries.
Descritores: Bacillus/metabolismo
Quitinases/metabolismo
-Fósforo/metabolismo
Temperatura
Bacillus/isolamento & purificação
Bacillus/genética
Bacillus/ultraestrutura
Estabilidade Enzimática/efeitos dos fármacos
Carbono/metabolismo
RNA Ribossômico 16S/genética
Cinética
Quitinases/química
Análise de Sequência de DNA
Ativação Enzimática
Concentração de Íons de Hidrogênio
Íons
Metais
Nitrogênio/metabolismo
Responsável: BR1.1 - BIREME


  5 / 29 LILACS  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
Texto completo
Id: biblio-963904
Autor: Devi, C. Subathra; Srinivasan, V. Mohana; Archana, B; Roy, Steffi Susan; Naine, S. Jemimah.
Título: Production and partial purification of antifungal chitinase from Bacillus cereus VITSD3
Fonte: Biosci. j. (Online);31(3):960-968, may./jun. 2015.
Idioma: en.
Resumo: The current work was designed to isolate and characterize chitin degrading bacteria. Among the 55 bacterial colonies isolated from 7 different soil samples, 4 isolates were capable of degrading chitinase, among which one strain VITSD3 was found to be potent. Based on the morphological, biochemical and molecular characterization of VITSD3 the isolate was confirmed as Bacillus cereus (Genbank accession number: KC961638), designated as Bacillus cereus VITSD3. The crude enzyme had a total activity of 220 U, precipitated with 44.8 U and 22.5 U for dialysed sample. The hydrolysed product NAG (N-Acetyl Glucosamine) from chitin was analysed by high-pressure liquid chromatography (HPLC).The molecular weight of the chitinase was determined using SDS PAGE and found to be 55 kDa. The partially purified chitinase produced from Bacillus cereus VITSD3 showed antifungal activity against Aspergillus fumigatus (18 mm), Aspergillus niger (6 mm) and Aspergillus flavus (15 mm). Hence the investigation suggests a potential benefit of partially purified chitinase extracted from Bacillus cereus VITSD3 which will serve as an excellent antifungal potential with therapeutic use.

O presente trabalho atual foi delineado para isolar e caracterizar bactérias degradadoras de quitina. Entre as 55 colónias bacterianas isoladas a partir de 7 amostras de solo diferentes, quatro isolados foram capazes de degradar quitinase, entre os quais uma estirpe, VITSD3, mostrou-se potente. Com base na caracterização morfológica, bioquímica e molecular de VIT D3 a soluto foi confirmada como Bacillus cereus (número de acesso Genbank: KC961638), designada como Bacillus cereus VITSD3. A enzima bruta tinha uma actividade total de 220 L, precipitou-se com 44,8 L e 22,5 L de amostra dialisada. O produto hidrolisado NAG (N-acetil-glucosamina) a partir de quitina foi analisado por cromatografia líquida de alta pressão (HPLC) .O peso molecular da quitinase foi determinado, utilizando-se SDS-PAGE e verificou-se ser 55 kDa. A quitinase parcialmente purificada produzida a partir de Bacillus cereus VITSD3 mostrou actividade antifúngica contra Aspergillus fumigatus (18 mm), Aspergillus niger (6 mm) e Aspergillus flavus (15 mm). Por isso, a investigação sugere um potencial benefício de quitinase parcialmente purificada extraída de Bacillus cereus VITSD3 o que poderá servir como um excelente potencial antifúngico para uso terapêutico.
Descritores: Aspergillus
Solo
Bacillus cereus
Quitina
Quitinases
Responsável: BR396.1 - Biblioteca Central


  6 / 29 LILACS  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo SciELO Brasil
Texto completo
Id: biblio-894899
Autor: Ortigão-Farias, João Ramalho; Di-Blasi, Tatiana; Telleria, Erich Loza; Andorinho, Ana Carolina; Lemos-Silva, Thais; Ramalho-Ortigão, Marcelo; Tempone, Antônio Jorge; Traub-Csekö, Yara Maria.
Título: Alternative splicing originates different domain structure organization of Lutzomyia longipalpis chitinases
Fonte: Mem. Inst. Oswaldo Cruz;113(2):96-101, Feb. 2018. graf.
Idioma: en.
Resumo: BACKGROUND The insect chitinase gene family is composed by more than 10 paralogs, which can codify proteins with different domain structures. In Lutzomyia longipalpis, the main vector of visceral leishmaniasis in Brazil, a chitinase cDNA from adult female insects was previously characterized. The predicted protein contains one catalytic domain and one chitin-binding domain (CBD). The expression of this gene coincided with the end of blood digestion indicating a putative role in peritrophic matrix degradation. OBJECTIVES To determine the occurrence of alternative splicing in chitinases of L. longipalpis. METHODS We sequenced the LlChit1 gene from a genomic clone and the three spliced forms obtained by reverse transcription polymerase chain reaction (RT-PCR) using larvae cDNA. FINDINGS We showed that LlChit1 from L. longipalpis immature forms undergoes alternative splicing. The spliced form corresponding to the adult cDNA was named LlChit1A and the two larvae specific transcripts were named LlChit1B and LlChit1C. The B and C forms possess stop codons interrupting the translation of the CBD. The A form is present in adult females post blood meal, L4 larvae and pre-pupae, while the other two forms are present only in L4 larvae and disappear just before pupation. Two bands of the expected size were identified by Western blot only in L4 larvae. MAIN CONCLUSIONS We show for the first time alternative splicing generating chitinases with different domain structures increasing our understanding on the finely regulated digestion physiology and shedding light on a potential target for controlling L. longipalpis larval development.
Descritores: Quitinases/genética
Reação em Cadeia da Polimerase Via Transcriptase Reversa
Sistema Digestório/enzimologia
-Quitinases/fisiologia
Processamento Alternativo/genética
Limites: Animais
Responsável: BR1.1 - BIREME


  7 / 29 LILACS  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
Texto completo
Id: biblio-914315
Autor: Rey, Maristela dos Santos; Beneman, Daiane de Pinho; Pinto, Luciano da S; Silva, Fabio Sérgio Paulino da; Braga, Eugenia Jacira B; Moura, Andréa B; Pierobom, Carlos Roberto; Peters, José A.
Título: Indução de resistência em arroz contra Bipolaris oryzae Breda de Hann, através da expressão constitutiva de um gene de quitinase / Induction of resistance in rice against Bipolaris oryzae Breda de Hann by constitutive expression of achitinase gene
Fonte: Biosci. j. (Online);28(5):745-752, sept./oct 2012. ilus, tab.
Idioma: pt.
Resumo: Este trabalho objetivou a transformação genética da cultivar de arroz BRS Taim, para obtenção de resistência ao fungo Bipolaris oryzae, agente da mancha parda. Para a transformação das plantas foi utilizada a cepa LBA 4404 de Agrobacterium tumefaciens transformada com o plasmídeo pMOG 22 que codifica o gene da quitinase do fungo entomopatogênico Metarhizium anisopliae. Mesocótilos de arroz foram imersos por 30 min. em solução bacteriana (OD600 = 0,7), contendo acetoceringona (100 Mm). Após os explantes foram co-cultivados por 72 horas em meio MS sem hormônio. Para seleção dos transformantes foi utilizado meio MS com 5 mg L-1 de BAP e 15 mg L-1 de higromicina, incubados a 25±1°C, fotoperíodo de 16 horas e densidade de fluxo de fótons de 42 µmol m-2 s-1. Foram obtidas 5 plantas transformadas, perfazendo uma média de eficiência de transformação de 1,53 %. A resistência das plantas foi observada somente por um dos isolados. Os resultados permitem concluir que as plantas de arroz transformadas com o gene da quitinase(Chit 1)podem reduzir o desenvolvimento do fungo B. oryzae, porém existe uma diferença na reação entre isolados.

This study aimed at a rice transformation for resistance to Bipolaris oryzae causal organism of Brown Spot, the cultivar BRS Taim and the line LBA 4404 of Agrobacterium tumefaciens transformed with plasmid pMOG 22 that codifies the chitinasegene Metarhizium anisopliae was used. Rice mesocotils immersed for 30 min in bacterial solution of OD600 = 0,7 with acetoceringone (100Mm), were co-cultivated for 72 hours in MS medium free of hormones and with 100Mm of acetoceringone. Mesocotils were then transferred to MS with 5mg L-1 de BAP and15 mg L-1 of higromicin for 45 days at 25°C and 16 ligth hours. The five transformed plants obtained (1,53 transformation rate) were inoculated with two B. oryzae isolates.Resistance was observed only with one of the isolates. The results indicate that rice plants transformed with chitinase gene (Chit 1)can reduce the colonization by some isolates of B. oryzae.
Descritores: Oryza
Transformação Genética
Quitinases
Fungos
Responsável: BR396.4


  8 / 29 LILACS  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Id: biblio-933582
Autor: Pereira, Sheila Tavares(aut).
Título: Estudo do Aedes aegypti considerando o processo de eclosão da forma imatura e o efeito da alimentação sanguínea e da infecção pelo Plasmodium gallinaceum no intestino médio do adulto.
Fonte: Campos dos Goytacazes; s.n; 2005. 83 p. ilus.
Idioma: pt.
Tese: Apresentada a Universidade Estadual do Norte Fluminense. Centro de Biociências e Biotecnologia para obtenção do grau de Doutor.
Descritores: Aedes
Quitinases
Plasmodium gallinaceum/microbiologia
Plasmodium gallinaceum/parasitologia
Responsável: BR1719.1 - Biblioteca do CPqRR
BR1719.1; 616.936 2 TE, P436s, 2005. 011318 011319


  9 / 29 LILACS  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo SciELO Brasil
Texto completo
Id: biblio-889234
Autor: Toufiq, Nida; Tabassum, Bushra; Bhatti, Muhammad Umar; Khan, Anwar; Tariq, Muhammad; Shahid, Naila; Nasir, Idrees Ahmad; Husnain, Tayyab.
Título: Improved antifungal activity of barley derived chitinase I gene that overexpress a 32 kDa recombinant chitinase in Escherichia coli host
Fonte: Braz. j. microbiol;49(2):414-421, Apr.-June 2018. tab, graf.
Idioma: en.
Resumo: Abstract Agricultural crops suffer many diseases, including fungal and bacterial infections, causing significant yield losses. The identification and characterisation of pathogenesis-related protein genes, such as chitinases, can lead to reduction in pathogen growth, thereby increasing tolerance against fungal pathogens. In the present study, the chitinase I gene was isolated from the genomic DNA of Barley (Hordeum vulgare L.) cultivar, Haider-93. The isolated DNA was used as template for the amplification of the ∼935 bp full-length chitinase I gene. Based on the sequence of the amplified gene fragment, class I barley chitinase shares 93% amino acid sequence homology with class II wheat chitinase. Interestingly, barley class I chitinase and class II chitinase do not share sequence homology. Furthermore, the amplified fragment was expressed in Escherichia coli Rosetta strain under the control of T7 promoter in pET 30a vector. Recombinant chitinase protein of 35 kDa exhibited highest expression at 0.5 mM concentration of IPTG. Expressed recombinant protein of 35 kDa was purified to homogeneity with affinity chromatography. Following purification, a Western blot assay for recombinant chitinase protein measuring 35 kDa was developed with His-tag specific antibodies. The purified recombinant chitinase protein was demonstrated to inhibit significantly the important phytopathogenic fungi Alternaria solani, Fusarium spp, Rhizoctonia solani and Verticillium dahliae compared to the control at concentrations of 80 µg and 200 µg.
Descritores: Antifúngicos/farmacologia
Quitinases/farmacologia
Hordeum/enzimologia
Proteínas Recombinantes/metabolismo
-Antifúngicos/química
Antifúngicos/isolamento & purificação
Western Blotting
Quitinases/química
Quitinases/genética
Quitinases/isolamento & purificação
Cromatografia de Afinidade
Escherichia coli/genética
Escherichia coli/metabolismo
Expressão Gênica
Hordeum/genética
Peso Molecular
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/isolamento & purificação
Homologia de Sequência de Aminoácidos
Responsável: BR1.1 - BIREME


  10 / 29 LILACS  
              first record previous record
seleciona
para imprimir
Fotocópia
Texto completo SciELO Brasil
Texto completo
Id: biblio-889152
Autor: Dhawan, Manish; Joshi, Neelam.
Título: Enzymatic comparison and mortality of Beauveria bassiana against cabbage caterpillar Pieris brassicae LINN
Fonte: Braz. j. microbiol;48(3):522-529, July-Sept. 2017. tab, graf.
Idioma: en.
Resumo: Abstract Beauveria bassiana, an entomopathogenic fungus, is the alternative biocontrol agent exploited against major economic crop pests. Pieris brassicae L. is an emerging pest of the Brassicaceae family. Therefore, in the present study, fungal isolates of Beauveria bassiana, viz. MTCC 2028, MTCC 4495, MTCC 6291, and NBAII-11, were evaluated for their virulence against third instar larvae of P. brassicae. Among all these fungal isolates, maximum mortality (86.66%) was recorded in B. bassiana MTCC 4495 at higher concentration of spores (109 conidia/ml), and the minimum mortality (30.00%) was recorded in B. bassiana MTCC 6291 at a lower concentration (107 conidia/ml) after ten days of treatment. The extracellular cuticle-degrading enzyme activities of fungal isolates were measured. Variability was observed both in the pattern of enzyme secretion and the level of enzyme activities among various fungal isolates. B. bassiana MTCC 4495 recorded the maximum mean chitinase (0.51 U/ml), protease (1.12 U/ml), and lipase activities (1.36 U/ml). The minimum mean chitinase and protease activities (0.37 and 0.91 U/ml, respectively) were recorded in B. bassiana MTCC 6291. The minimum mean lipase activity (1.04 U/ml) was recorded in B. bassiana NBAII-11. Our studies revealed B. bassiana MTCC 4495 as the most pathogenic isolate against P. brassicae, which also recorded maximum extracellular enzyme activities, suggesting the possible roles of extracellular enzymes in the pathogenicity of B. bassiana against P. brassicae.
Descritores: Beauveria/enzimologia
Beauveria/patogenicidade
Brassica/parasitologia
Quitinases/metabolismo
Proteínas Fúngicas/metabolismo
Mariposas/microbiologia
Controle Biológico de Vetores/métodos
Doenças das Plantas/parasitologia
-Beauveria/genética
Quitinases/genética
Proteínas Fúngicas/genética
Larva/microbiologia
Larva/fisiologia
Mariposas/fisiologia
Virulência
Limites: Animais
Tipo de Publ: Estudo Comparativo
Estudo de Avaliação
Responsável: BR1.1 - BIREME



página 1 de 3 ir para página          
   


Refinar a pesquisa
  Base de dados : Formulário avançado   

    Pesquisar no campo  
1  
2
3
 
           



Search engine: iAH v2.6 powered by WWWISIS

BIREME/OPAS/OMS - Centro Latino-Americano e do Caribe de Informação em Ciências da Saúde