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1.
Bull Tokyo Dent Coll ; 55(1): 19-23, 2014.
Artigo em Inglês | MEDLINE | ID: mdl-24717926

RESUMO

A new semi-quantitative enumeration system has been developed for the detection of Streptococcus mutans in saliva. Using two kinds of species-specific monoclonal antibodies, this system can quickly detect salivary S. mutans within 30 min and classify the results into three levels. The aim of this study was to evaluate the potential of this test kit in determining risk for the development of caries. Saliva samples collected during a compulsory dental examination from 56 children aged 18-months were tested. The children were classified into 3 groups according to the level of salivary S. mutans determined. After 18 months, 36 of the children underwent a second examination to investigate whether there was a correlation between salivary S. mutans level at the first examination and subsequent increment in caries. The results showed a good correlation between the two. This indicates that salivary S. mutans level before the window of infection is an indicator of caries risk and can be quickly detected using this test kit. This rapid test should be particularly useful in assessing risk of future caries in very young children.


Assuntos
Anticorpos Monoclonais/imunologia , Suscetibilidade à Cárie Dentária/fisiologia , Cárie Dentária/etiologia , Saliva/microbiologia , Streptococcus mutans/isolamento & purificação , Carga Bacteriana , Índice CPO , Cárie Dentária/microbiologia , Feminino , Seguimentos , Previsões , Humanos , Lactente , Masculino , Kit de Reagentes para Diagnóstico , Medição de Risco , Especificidade da Espécie , Streptococcus mutans/imunologia
2.
Protein J ; 26(3): 153-8, 2007 Apr.
Artigo em Inglês | MEDLINE | ID: mdl-17203392

RESUMO

The similarity between the structural scaffold of PQQGDH and that of sialidase in the absence of any similarity in the primary structure, catalytic function and substrate recognition encouraged us to attempt a W-motif exchange between these enzymes. By substituting one W-motif in PQQGDH with one from sialidase, a chimeric PQQGDH was constructed, and its enzymatic properties were investigated. The overexpression of the chimeric enzyme resulted in the formation of an inclusion body. However, the refolding procedure resulted in a soluble chimeric enzyme with PQQGDH activity showing similar secondary-structure components as native PQQGDH. In contrast to native PQQGDH, the chimeric PQQGDH showed thermal instability and sensitivity to EDTA; this difference might have been due to the incomplete compatibility of the inserted W-motif. The potential of W-motif replacement was also discussed in view of the possible molecular evolution/engineering of beta-propeller structures.


Assuntos
Glucose Desidrogenase/química , Neuraminidase/química , Motivos de Aminoácidos , Sequência de Aminoácidos , Domínio Catalítico , Modelos Biológicos , Dados de Sequência Molecular , Engenharia de Proteínas , Dobramento de Proteína , Proteínas Recombinantes de Fusão/química , Proteínas Recombinantes de Fusão/genética , Proteínas Recombinantes de Fusão/metabolismo , Relação Estrutura-Atividade
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