Home Itens selecionados Provedores de dados OAI Créditos Sobre Ajuda

			Busca avançada
	Provedor de dados 56 (2) Autor Thedei Jr.,G. (2) Bolean,M. (1) Ciancaglini,P. (1) Leitão,D.P.S. (1) Maccheroni Jr.,W. (1) Morales,A.C. (1) Nozawa,S.R. (1) Paulino,T.P. (1) Rossi,A. (1) Spadaro,A.C.C. (1) Mais... Palavra-chave Alkaline phosphatase (1) Cell permeabilization (1) F-type ATPase (1) Fungi (1) L-histidinol-Pi phosphatase (1) Neurospora crassa (1) P-type ATPase (1) Streptococcus mutans (1) Toluene permeabilization (1) Mais... Tipo do documento Info:eu-repo/semantics/article (2) Ano 2008 (1) 2000 (1) País Brazil (2) Idioma Inglês (2)		Ordenar por:  Relevância Autor Título Ano Registros recuperados: 2 Primeira ... 1 ... Última Toluene permeabilization differentially affects F- and P-type ATPase activities present in the plasma membrane of Streptococcus mutans 56 Thedei Jr.,G.; Leitão,D.P.S.; Bolean,M.; Paulino,T.P.; Spadaro,A.C.C.; Ciancaglini,P.. Streptococcus mutans membrane-bound P- and F-type ATPases are responsible for H+ extrusion from the cytoplasm thus keeping intracellular pH appropriate for cell metabolism. Toluene-permeabilized bacterial cells have long been used to study total membrane-bound ATPase activity, and to compare the properties of ATPase in situ with those in membrane-rich fractions. The aim of the present research was to determine if toluene permeabilization can significantly modify the activity of membrane-bound ATPase of both F-type and P-type. ATPase activity was assayed discontinuously by measuring phosphate release from ATP as substrate. Treatment of S. mutans membrane fractions with toluene reduced total ATPase activity by approximately 80% and did not allow... Tipo: Info:eu-repo/semantics/article Palavras-chave: Cell permeabilization; F-type ATPase; P-type ATPase; Toluene permeabilization; Streptococcus mutans. Ano: 2008 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2008001200002 Properties of a constitutive alkaline phosphatase from strain 74A of the mold Neurospora crassa 56 Morales,A.C.; Nozawa,S.R.; Thedei Jr.,G.; Maccheroni Jr.,W.; Rossi,A.. A constitutive alkaline phosphatase was purified to apparent homogeneity as determined by polyacrylamide gel electrophoresis from mycelia of the wild strain 74A of the mold Neurospora crassa, after growth on acetate and in the presence of saturating amounts of inorganic phosphate (Pi) for 72 h at 30ºC. The molecular mass was 58 kDa and 56 kDa as determined by exclusion chromatography and SDS-PAGE, respectively. This monomeric enzyme shows an apparent optimum pH ranging from 9.5 to 10.5 and Michaelis kinetics for the hydrolysis of p-nitrophenyl phosphate (the Km and Hill coefficient values were 0.35 mM and 1.01, respectively), alpha-naphthyl phosphate (the Km and Hill coefficient values were 0.44 mM and 0.97, respectively), ß-glycerol phosphate (the Km and... Tipo: Info:eu-repo/semantics/article Palavras-chave: Neurospora crassa; Fungi; Alkaline phosphatase; L-histidinol-Pi phosphatase. Ano: 2000 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2000000800006 Registros recuperados: 2 Primeira ... 1 ... Última

Empresa Brasileira de Pesquisa Agropecuária - Embrapa Todos os direitos reservados, conforme Lei n° 9.610 Política de Privacidade Área restrita		Embrapa Parque Estação Biológica - PqEB s/n° Brasília, DF - Brasil - CEP 70770-901 Fone: (61) 3448-4433 - Fax: (61) 3448-4890 / 3448-4891 SAC: https://www.embrapa.br/fale-conosco