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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


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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


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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


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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


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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


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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
Estudos de Avaliação
Responsável: BR1.1 - BIREME


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Id: biblio-839234
Autor: Thimoteo, SS; Glogauer, A; Faoro, H; de Souza, EM; Huergo, LF; Moerschbacher, BM; Pedrosa, FO.
Título: A broad pH range and processive chitinase from a metagenome library
Fonte: Braz. j. med. biol. res = Rev. bras. pesqui. méd. biol;50(1):e5658, 2017. tab, graf.
Idioma: en.
Projeto: INCT-FBN/CNPq/MCT.
Resumo: Chitinases are hydrolases that degrade chitin, a polymer of N-acetylglucosamine linked β(1-4) present in the exoskeleton of crustaceans, insects, nematodes and fungal cell walls. A metagenome fosmid library from a wastewater-contaminated soil was functionally screened for chitinase activity leading to the isolation and identification of a chitinase gene named metachi18A. The metachi18A gene was subcloned and overexpressed in Escherichia coli BL21 and the MetaChi18A chitinase was purified by affinity chromatography as a 6xHis-tagged fusion protein. The MetaChi18A enzyme is a 92-kDa protein with a conserved active site domain of glycosyl hydrolases family 18. It hydrolyses colloidal chitin with an optimum pH of 5 and temperature of 50°C. Moreover, the enzyme retained at least 80% of its activity in the pH range from 4 to 9 and 98% at 600 mM NaCl. Thin layer chromatography analyses identified chitobiose as the main product of MetaChi18A on chitin polymers as substrate. Kinetic analysis showed inhibition of MetaChi18A activity at high concentrations of colloidal chitin and 4-methylumbelliferyl N,N′-diacetylchitobiose and sigmoid kinetics at low concentrations of colloidal chitin, indicating a possible conformational change to lead the chitin chain from the chitin-binding to the catalytic domain. The observed stability and activity of MetaChi18A over a wide range of conditions suggest that this chitinase, now characterized, may be suitable for application in the industrial processing of chitin.
Descritores: Quitinases/genética
Quitina/genética
Metagenoma/genética
-Quitinases/química
Quitina/química
Cromatografia Líquida de Alta Pressão
Escherichia coli
Expressão Gênica/genética
Biblioteca Gênica
Vetores Genéticos
Concentração de Íons de Hidrogênio
Especificidade por Substrato
Responsável: BR1.1 - BIREME


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Id: lil-775113
Autor: Rao, K.L.N Mallikharjuna; Raju, K. Siva; Ravisankar, H..
Título: Cultural conditions on the production of extracellular enzymes by Trichoderma isolates from tobacco rhizosphere
Fonte: Braz. j. microbiol;47(1):25-32, Jan.-Mar. 2016. tab, graf.
Idioma: en.
Resumo: Abstract Twelve isolates of Trichoderma spp. isolated from tobacco rhizosphere were evaluated for their ability to produce chitinase and β-1,3-glucanase extracellular hydrolytic enzymes. Isolates ThJt1 and TvHt2, out of 12 isolates, produced maximum activities of chitinase and β-1,3-glucanase, respectively. In vitro production of chitinase and β-1,3-glucanase by isolates ThJt1 and TvHt2 was tested under different cultural conditions. The enzyme activities were significantly influenced by acidic pH and the optimum temperature was 30 °C. The chitin and cell walls of Sclerotium rolfsii, as carbon sources, supported the maximum and significantly higher chitinase activity by both isolates. The chitinase activity of isolate ThJt1 was suppressed significantly by fructose (80.28%), followed by glucose (77.42%), whereas the β-1,3-glucanase activity of ThJt1 and both enzymes of isolate TvHt2 were significantly suppressed by fructose, followed by sucrose. Ammonium nitrate as nitrogen source supported the maximum activity of chitinase in both isolates, whereas urea was a poor nitrogen source. Production of both enzymes by the isolates was significantly influenced by the cultural conditions. Thus, the isolates ThJt1 and TvHt2 showed higher levels of chitinase and β-1,3-glucanase activities and were capable of hydrolyzing the mycelium of S. rolfsii infecting tobacco. These organisms can be used therefore for assessment of their synergism in biomass production and biocontrol efficacy and for their field biocontrol ability against S. rolfsii and Pythium aphanidermatum infecting tobacco.
Descritores: Quitinases
GLUCAN 1,ABATTOIRS-BETA-GLUCOSIDASE/ECRET
Microbiologia do Solo
Trichoderma/enzimologia
Trichoderma/crescimento & desenvolvimento
-Basidiomycota/metabolismo
Carbono/metabolismo
Parede Celular/metabolismo
Quitina/metabolismo
Meios de Cultura/química
Concentração de Íons de Hidrogênio
Nitrogênio/metabolismo
Rizosfera
Temperatura Ambiente
Tabaco
Trichoderma/isolamento & purificação
Responsável: BR1.1 - BIREME


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Id: lil-769641
Autor: Asad, Saeed Ahmad; Tabassum, Ayesha; Hameed, Abdul; Hassan, Fayyaz ul; Afzal, Aftab; Khan, Sabaz Ali; Ahmed, Rafiq; Shahzad, Muhammad.
Título: Determination of lytic enzyme activities of indigenous Trichoderma isolates from Pakistan
Fonte: Braz. j. microbiol;46(4):1053-1064, Oct.-Dec. 2015. tab, graf.
Idioma: en.
Resumo: Abstract This study investigated lytic enzyme activities in three indigenous Trichoderma strains namely, Trichoderma asperellum, Trichoderma harzianum and Trichoderma sp. Native Trichoderma strains and a virulent strain of Rhizoctonia solani isolated from infected bean plants were also included in the study. Enzyme activities were determined by measuring sugar reduction by dinitrosalicylic acid (DNS) method using suitable substrates. The antagonists were cultured in minimal salt medium with the following modifications: medium A (1 g of glucose), medium B (0.5 g of glucose + 0.5 g of deactivated R. solani mycelia), medium C (1.0 g of deactivated respective antagonist mycelium) and medium D (1 g of deactivated R. solani mycelia). T asperellum showed presence of higher amounts of chitinases, β-1, 3-glucanases and xylanases in extracellular protein extracts from medium D as compared to medium A. While, the higher activities of glucosidases and endoglucanses were shown in medium D extracts by T. harzianum. β-glucosidase activities were lower compared with other enzymes; however, activities of the extracts of medium D were significantly different. T. asperellum exhibited maximum inhibition (97.7%). On the other hand, Trichoderma sp. did not show any effect on mycelia growth of R. solani on crude extract.
Descritores: Quitinases/análise
Quitinases/química
Quitinases/enzimologia
Quitinases/crescimento & desenvolvimento
Quitinases/metabolismo
/análise
ENDO-1,ABBREVIATIONS AS TOPIC-BETA XYLANASES/análise
/química
ENDO-1,ABBREVIATIONS AS TOPIC-BETA XYLANASES/química
/enzimologia
ENDO-1,ABBREVIATIONS AS TOPIC-BETA XYLANASES/enzimologia
/crescimento & desenvolvimento
ENDO-1,ABBREVIATIONS AS TOPIC-BETA XYLANASES/crescimento & desenvolvimento
/metabolismo
ENDO-1,ABBREVIATIONS AS TOPIC-BETA XYLANASES/metabolismo
Proteínas Fúngicas/análise
Proteínas Fúngicas/química
Proteínas Fúngicas/enzimologia
Proteínas Fúngicas/crescimento & desenvolvimento
Proteínas Fúngicas/metabolismo
Glicosídeo Hidrolases/análise
Glicosídeo Hidrolases/química
Glicosídeo Hidrolases/enzimologia
Glicosídeo Hidrolases/crescimento & desenvolvimento
Glicosídeo Hidrolases/metabolismo
Micélio/análise
Micélio/química
Micélio/enzimologia
Micélio/crescimento & desenvolvimento
Micélio/metabolismo
Paquistão/análise
Paquistão/química
Paquistão/enzimologia
Paquistão/crescimento & desenvolvimento
Paquistão/metabolismo
Trichoderma/análise
Trichoderma/química
Trichoderma/enzimologia
Trichoderma/crescimento & desenvolvimento
Trichoderma/metabolismo
Responsável: BR1.1 - BIREME


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Id: lil-732595
Autor: Robles-Murguia, Maricela; Bloedow, Nicholas; Murray, Leigh; Ramalho-Ortigão, Marcelo.
Título: Effect of mouse antisera targeting the Phlebotomus papatasi midgut chitinase PpChit1 on sandfly physiology and fitness
Fonte: Mem. Inst. Oswaldo Cruz;109(8):1064-1069, 12/2014. tab.
Idioma: en.
Projeto: NIH RO1.
Resumo: In sandflies, the absence of the peritrophic matrix (PM) affects the rate of blood digestion. Also, the kinetics of PM secretion varies according to species. We previously characterised PpChit1, a midgut-specific chitinase secreted in Phlebotomus papatasi (PPIS) that is involved in the maturation of the PM and showed that antibodies against PpChit1 reduce the chitinolytic activity in the midgut of several sandfly species. Here, sandflies were fed on red blood cells reconstituted with naïve or anti-PpChit1 sera and assessed for fitness parameters that included blood digestion, oviposition onset, number of eggs laid, egg bouts, average number of eggs per bout and survival. In PPIS, anti-PpChit1 led to a one-day delay in the onset of egg laying, with flies surviving three days longer compared to the control group. Anti-PpChit1 also had a negative effect on overall ability of flies to lay eggs, as several gravid females from all three species were unable to lay any eggs despite having lived longer than control flies. Whereas the longer survival might be associated with improved haeme scavenging ability by the PM, the inability of females to lay eggs is possibly linked to changes in PM permeability affecting nutrient absorption.
Descritores: Quitinases/imunologia
Soros Imunes
Fatores Imunológicos/farmacologia
Proteínas de Insetos/efeitos dos fármacos
Insetos Vetores/efeitos dos fármacos
Phlebotomus/efeitos dos fármacos
-Quitinases
DNA Complementar
Digestão/efeitos dos fármacos
Comportamento Alimentar
Absorção Gastrointestinal/efeitos dos fármacos
Hemoglobinas
Soros Imunes/imunologia
Proteínas de Insetos
Insetos Vetores/fisiologia
Camundongos Endogâmicos BALB C
Controle de Mosquitos/métodos
Oviposição/efeitos dos fármacos
Plasmídeos
Phlebotomus/fisiologia
Limites: Animais
Feminino
Masculino
Tipo de Publ: Research Support, N.I.H., Extramural
Responsável: BR1.1 - BIREME



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