Your browser doesn't support javascript.
loading
Mostrar: 20 | 50 | 100
Resultados 1 - 2 de 2
Filtrar
Mais filtros











Intervalo de ano de publicação
1.
Appl Microbiol Biotechnol ; 84(5): 917-26, 2009 Oct.
Artigo em Inglês | MEDLINE | ID: mdl-19440704

RESUMO

Aspergillus nidulans produces StcI esterase, which is involved in the biosynthesis of sterigmatocystin, a precursor of aflatoxins. Previous reports of this esterase in A. nidulans suggest that it is composed of 286 amino acid residues with a theoretical molecular mass of 31 kDa. Various conditions were evaluated to determine the optimal expression conditions for StcI; the highest level was observed when A. nidulans was cultured in solid oat media. Various esterases were expressed differentially according to the culture media used. However, specific antibodies designed to detect StcI reacted with a protein with an unexpected molecular mass of 35 kDa in cell extracts from all expression conditions. Analysis of the gene sequence and already reported expressed sequence tags indicated the presence of an additional 29-amino-acid N-terminal region of StcI, which is not a signal peptide and which has not been previously reported. We also detected the presence of this additional N-terminal region using reverse-transcriptase polymerase chain reaction. The complete protein (NStcI) was cloned and successfully expressed in Pichia pastoris.


Assuntos
Aspergillus nidulans/enzimologia , Esterases/genética , Proteínas Fúngicas/genética , Sequência de Aminoácidos , Aspergillus nidulans/química , Aspergillus nidulans/genética , Sequência de Bases , Clonagem Molecular , Esterases/química , Esterases/metabolismo , Proteínas Fúngicas/química , Proteínas Fúngicas/metabolismo , Fungos/química , Fungos/classificação , Fungos/genética , Dados de Sequência Molecular , Peso Molecular , Filogenia , Alinhamento de Sequência
2.
Arch. med. res ; 24(1): 7-11, mar. 1993. tab
Artigo em Inglês | LILACS | ID: lil-176998

RESUMO

The present study describes the first attempt to detect antisecretory activity in a lectin fraction of plasma from patients with acute diarrhea. The plasma antisecretory protein (ASP) was purified by affinity chromatography in agarose, and its antisecretory activity in rats subjected to intestinal challenge with cholera toxin. During the first 24 h of the diarrheal episode, antisecretory activity in patients (median 0, range 0 -25 percent) was lower than that seen in the asymptomatic group (median 10, range 0 -30 percent); 3 days leter, when diarrhea ceased in most of the patients, the ASP activity increased significantly (median 30, range 0 -70 percent). However, 5 days later the activity decreased again (median 0, range 0 . 55 percent). No differences in ASP levels were found between cases associated with an enteropathogen and those whwew no pathogen was identified. These findings reveal an inverse relationship between the increase in ASP and the patient's intestinal secretion; suggesting that ASP plays a role in the compensatory mechanisms that occur in diarrhea in humans


Assuntos
Humanos , Masculino , Feminino , Pré-Escolar , Adolescente , Toxinas Bacterianas/metabolismo , Diarreia/enzimologia , Mucosa Intestinal/fisiopatologia , Secreções Intestinais/metabolismo , Lectinas , Proteínas Sanguíneas/análise
SELEÇÃO DE REFERÊNCIAS
DETALHE DA PESQUISA