Base de dados : LILACS
Pesquisa : G02.111.833 [Categoria DeCS]
Referências encontradas : 4 [refinar]
Mostrando: 1 .. 4   no formato [Detalhado]

página 1 de 1

  1 / 4 LILACS  
              next record last record
seleciona
para imprimir
Fotocópia
Texto completo SciELO Venezuela
Texto completo
Id: lil-517666
Autor: Mesa C., Luz Mila; Díaz, Marynes; Ocampo, Paola; Rodríguez De Valero, Sofía; Larrazabal, Marvelys; Guerra, Paula; León de Pinto, Gladys.
Título: Comparación del crecimiento de Malassezia furfur y Malassezia slooffiae en los medios del exudado gomoso de spondias dulcis y dixon / Comparison of the growth of Malassezia furfur and Malassezia slooffiae on spondias dulcis gum exudate and dixon media
Fonte: Kasmera;36(1):45-52, ene.-jun. 2008. graf, tab.
Idioma: es.
Resumo: Las levaduras del género Malassezia son hongos que producen afecciones en la piel. El desarrollo de estos microorganismos requiere condiciones especiales. El medio Dixon es generalmente usado para su cultivo. Se ensayo el exudado gomoso de Spondias dulcis como sustrato para Malassezia furfur y Malassezia slooffiae en comparación con el medio Dixon. Se determino la cinética de crecimiento a un determinado rango de tiempo (0-120h), a diferentes concentraciones (1,2 por ciento) y pH (4,0;6,0;7,0). La relativa alta biomasa obtenida para las dos levaduras probadas demostró que el sustrato preparado con el exudado gomoso de S. dulcis es adecuado para su desarrollo. Spondias dulcis especie localizada en Venezuela produce abundante goma. Este hecho, y los resultados obtenidos podría ser útil para preparar un nuevo sustrato que pueda competir con Dixon para el aislamiento y la caracterización de especies de Malassezia.

Malassezia yeasts are fungi that produce skin affections. Growth of these microorganisms requires specific conditions. The Dixon medium has generally been used for their culture and has been tested. The use of Spondias gum as a substrate for Malassezia furfur and Malassezia slooffiae was tried and compared with the Dixon medium. The growth kinetic for a given time range(0-120 h) was determined at different concentrations (1.2 percent) and pH levels (4,0; 6,0;7,0). The relatively high biomass obtained for the two tested yeasts demonstrated that the substrate prepared with S. dulcis gum exudate is suitable for their growth. Spondias dulcis, a species located in Venezuela, yields abundant gum. This fact and the results discussed above indicate that it could be used to prepare a substrate that could compete with Dixon for isolating and characterizing the Malassezia species.
Descritores: Anacardiaceae
Malassezia
Dermatopatias Infecciosas
Ciclização de Substratos
Tipo de Publ: Revisão
Responsável: VE1.1 - Biblioteca Humberto Garcia Arocha


  2 / 4 LILACS  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Id: lil-216824
Autor: Turnes, Rosario Elena; Bahar, Susan.
Título: Production of cyclomaltodextrin glucanotransferase from an alkalophilic Bacillus sp. in rice and corn flakes
Fonte: Acta cient. venez;47(2):133-7, 1996. tab, graf.
Idioma: en.
Resumo: Cyclomaltodextrin glucanotranferase (CGTase) catalyzes the degradation of starch to form alpha-, beta- and gamma-cyclodextrin. Based on cyclodextrin formation, an alkalophilic Bacillus sp. ATCC 21783 was used for its high CGTase production ability, using corn and rice flakes as substrates. Maximum enzyme production was achieved after 96 hours at pH 9.0, temperature 37 degrees C, and 1 percent(w/v) of either substrate together with the addition of trub. The specific enzyme activity was determined by High Pressure Liquid Chromatography (HPLC) and expressed as using International Units based on total cyclodextrin formation. Optimum conditions for this determination were studied, finding that the best results are obtained at pH 5.0, 7.0 and 9.0, temperature 55 degrees C and 3 hours of incubation in 1 percent (w/v) of rice flakes as starch source
Descritores: Bacillus/enzimologia
Glucosiltransferases/biossíntese
-Oryza
Ciclização de Substratos
Zea mays
Responsável: BR1.1 - BIREME


  3 / 4 LILACS  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Id: lil-163839
Autor: Sousa, M. O; Rodrigues, C. V; Pena, H. B; Alvarenga, M. G; Machado-Coelho, G. L. L; Santoro, M. M; Juliano, M. A; Juliano, L; Figueiredo, A. F. S.
Título: Kinetic characterization of rat tissue kallikrein using NÓ-substituted arginine 4-nitroanilides and NÓ-benzoyl-L-arginine ethyl ester as substrates
Fonte: Braz. j. med. biol. res = Rev. bras. pesqui. méd. biol;29(3):327-34, Mar. 1996. tab, graf.
Idioma: en.
Conferência: Apresentado em: Annual Meeting of the Brazilian Society of Biochemistry and Molecular Biology, 22, Caxambu, May 1-4, 1993.
Resumo: Hydrolysis of seven N(alpha-substituted L-arginine 4-nitroanilides: henzoyl-arginine p-nitroanilide (Bz-Arg-Nan), tosyl-arginine p-nitroanilide (Tos-Arg-Nan), acetyl-leucyl-arginine p-nitroanilide (Ac-Leu-Arg-Nan), acetyl-phenylalanyl-arginine p-nitroanilide (Ac-Phe-Arg-Nan), benzoyl-phenylalanyl-arginine p-nitroanilide (Bz-Phe-Arg-Nan), tosyl-phenylalanyl-arginine p-nitroanilide (Tos-Phe-Arg-Nan), and D-valyl-leucyl-arginine p-nitroanilide (D-Val-Leu-Arg-Nan), and the N(alpha-substituted L-arginine ester: benzoyl-arginine ethyl ester (Bz-Arg-OEt), by rat tissue kallikrein was studied throughout a wide range of substrate concentrations. The enzyme showed a bimodal behavior with all the substrates tested except Tos-Arg-Nan. At low substrate concentrations (10 to 170 muM for p-nitroanilides and 50 to 190 muM for Bz-Arg-OEt) the hydrolysis followed Michaelis-Menten kinetics, but at higher substrate concentrations (150 to 700 muM for p-nitroanilides and 200 to 1800 muM for Bz-Arg-OEt) a deviation from Michaelis-Menten kinetics was observed with a significant decrease in hydrolysis rates. At high concentrations of the p-nitroanilide substrates, partial enzyme inhibition was observed, whereas complete enzyme inhibition was observed with Bz-Arg-OEt at high concentration. The kinetic parameters reported here were calculated from data for substrate concentrations range where the enzyme followed Michaelis-Menten behavior. D-Val-Leu-Arg-Nan (Km = 24 ñ 2 muM; Vmax 10.42 ñ 0.28 muM/min) was the best substrate tested, followed by Ac-Phe-Arg-Nan (Km = 13 ñ 2 muM; Vmax = 3.21 ñ 0.11 muM/min), while Tos-Arg-Nan (Km = 29 ñ 2 muM; Vmax, = 0. 10 ñ 0.002 muM/min) was the worst of the tested substrates for rat tissue kallikrein. For the hydrolysis of Bz-Arg-OEt (Km = 125 ñ 15 muM; Vmax = 121.3 ñ 7.6 muM/min), the kinetic parameters using a substrate inhibition model can reasonably account for the observed enzyme behavior, with a Ksi value about 13.6 times larger than the estimated Km value.
Descritores: Arginina/metabolismo
Calicreínas/farmacocinética
-Calicreínas/isolamento & purificação
Calicreínas/urina
Hidrólise
Ciclização de Substratos
Limites: Animais
Ratos
Responsável: BR1.1 - BIREME


  4 / 4 LILACS  
              first record previous record
seleciona
para imprimir
Fotocópia
Id: lil-75673
Autor: Mildvan, Albert S.
Título: Nuclear relaxation and Overhauser effect studies of enzyme-substrate interactions
Fonte: Arch. biol. med. exp;22(2):147-51, jul. 1989. ilus.
Idioma: en.
Projeto: National Institutes of Health; . National Science Foundation.
Descritores: Enzimas/metabolismo
Proteínas/metabolismo
Ciclização de Substratos/efeitos da radiação
Tipo de Publ: Revisão
Responsável: CL1.1 - Biblioteca Central



página 1 de 1
   


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