Rev. Otorrinolaringol. Cir. Cabeza Cuello 2009; 69: 271-280,
Oscar Cañete S1.
1 Tecnólogo Médico, Servicio de Otorrinolaringología, Hospital Padre Hurtado.
Palabras clave: Neuropatía auditiva, des sincronía auditiva, desorden del espectro de neuropatía auditiva, hipoacusia neural, hipoacusia en neonatos de riesgo, potenciales evocados de tronco, ataxia de Friedreich, Charcot-Marie-Tooth.
Keywords: Auditory neuropathy, Neural hearing loss, Auditory evoked potentials, Auditory Dyssynchrony. Hearing loss in high risk newborns, Friedreich's ataxia, Charcot-Marie-Tooth.
FULL TEXT (Spanish)
Tuesday, February 2, 2010
Rapid determination of tricarboxylic acid cycle enzyme activities in biological samples
BMC Biochemistry 2010, 11:5doi:10.1186/1471-2091-11-5
Sergio Goncalves , Vincent Paupe , Emmanuel P Dassa , Jean-Jacques Briere , Judith Favier , Anne-Paule Gimenez-Roqueplo , Paule Benit and Pierre Rustin
Published: 28 January 2010
OPEN ACCES
Abstract (provisional)
Background
In the last ten years, deficiencies in tricarboxylic acid cycle (TCAC) enzymes have been shown to cause a wide spectrum of human diseases, including malignancies and neurological and cardiac diseases. A prerequisite to the identification of disease-causing TCAC enzyme deficiencies is the availability of effective enzyme assays.
Results
We developed three assays that measure the full set of TCAC enzymes. One assay relies on the sequential addition of reagents to measure succinyl-CoA ligase activity, followed by succinate dehydrogenase, fumarase and, finally, malate dehydrogenase. Another assay measures the activity of -ketoglutarate dehydrogenase followed by aconitase and isocitrate dehydrogenase. The remaining assay measures citrate synthase activity using a standard procedure. We used these assays successfully on extracts of small numbers of human cells displaying various severe or partial TCAC deficiencies and on frozen heart homogenates from heterozygous mice harboring an SDHB gene deletion.
Conclusion
This set of assays is rapid and simple to use and can immediately detect even partial defects, as the activity of each enzyme can be readily compared with one or more other activities measured in the same sample.
FULL TEXT (pdf)
Sergio Goncalves , Vincent Paupe , Emmanuel P Dassa , Jean-Jacques Briere , Judith Favier , Anne-Paule Gimenez-Roqueplo , Paule Benit and Pierre Rustin
Published: 28 January 2010
OPEN ACCES
Abstract (provisional)
Background
In the last ten years, deficiencies in tricarboxylic acid cycle (TCAC) enzymes have been shown to cause a wide spectrum of human diseases, including malignancies and neurological and cardiac diseases. A prerequisite to the identification of disease-causing TCAC enzyme deficiencies is the availability of effective enzyme assays.
Results
We developed three assays that measure the full set of TCAC enzymes. One assay relies on the sequential addition of reagents to measure succinyl-CoA ligase activity, followed by succinate dehydrogenase, fumarase and, finally, malate dehydrogenase. Another assay measures the activity of -ketoglutarate dehydrogenase followed by aconitase and isocitrate dehydrogenase. The remaining assay measures citrate synthase activity using a standard procedure. We used these assays successfully on extracts of small numbers of human cells displaying various severe or partial TCAC deficiencies and on frozen heart homogenates from heterozygous mice harboring an SDHB gene deletion.
Conclusion
This set of assays is rapid and simple to use and can immediately detect even partial defects, as the activity of each enzyme can be readily compared with one or more other activities measured in the same sample.
FULL TEXT (pdf)
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