S-Adenosyl methionine/S-adenosyl-L-homocysteine ratio determination by capillary electrophoresis employed as a monitoring tool for the antiviral effectiveness of adenosine analogs

S‐Adenosyl‐L‐homocysteine hydrolase (SAHh) inhibitors have long been used as broad‐range antivirals and have been recently evaluated as an experimental therapy of filovirus infections. In response to the need for a rapid laboratory testing method that could assess antiviral potency in vivo, our grou...

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Published inElectrophoresis Vol. 25; no. 10-11; pp. 1518 - 1521
Main Authors Sbrana, Elena, Bramanti, Emilia, Spinetti, Maria C., Raspi, Giorgio
Format Journal Article
LanguageEnglish
Published Weinheim WILEY-VCH Verlag 01.06.2004
WILEY‐VCH Verlag
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Abstract S‐Adenosyl‐L‐homocysteine hydrolase (SAHh) inhibitors have long been used as broad‐range antivirals and have been recently evaluated as an experimental therapy of filovirus infections. In response to the need for a rapid laboratory testing method that could assess antiviral potency in vivo, our group developed a capillary electrophoresis (CE) method for the determination of the S‐adenosyl‐L‐homocysteine (SAH) to S‐adenosyl‐L‐methionine (SAM) ratio. After chloroacetaldehyde derivatization, SAH and SAM were detected using laser‐induced fluorescence detection with a HeCd laser. Separation and quantitation of both SAH and SAM in human plasma were achieved in less than 1 min. The proposed method is rapid and reliable, and could be easily applied to routine monitoring of clinical and preclinical trials subjects.
AbstractList S-Adenosyl-L-homocysteine hydrolase (SAHh) inhibitors have long been used as broad-range antivirals and have been recently evaluated as an experimental therapy of filovirus infections. In response to the need for a rapid laboratory testing method that could assess antiviral potency in vivo, our group developed a capillary electrophoresis (CE) method for the determination of the S-adenosyl-L-homocysteine (SAH) to S-adenosyl-L-methionine (SAM) ratio. After chloroacetaldehyde derivatization, SAH and SAM were detected using laser-induced fluorescence detection with a HeCd laser. Separation and quantitation of both SAH and SAM in human plasma were achieved in less than 1 min. The proposed method is rapid and reliable, and could be easily applied to routine monitoring of clinical and preclinical trials subjects.S-Adenosyl-L-homocysteine hydrolase (SAHh) inhibitors have long been used as broad-range antivirals and have been recently evaluated as an experimental therapy of filovirus infections. In response to the need for a rapid laboratory testing method that could assess antiviral potency in vivo, our group developed a capillary electrophoresis (CE) method for the determination of the S-adenosyl-L-homocysteine (SAH) to S-adenosyl-L-methionine (SAM) ratio. After chloroacetaldehyde derivatization, SAH and SAM were detected using laser-induced fluorescence detection with a HeCd laser. Separation and quantitation of both SAH and SAM in human plasma were achieved in less than 1 min. The proposed method is rapid and reliable, and could be easily applied to routine monitoring of clinical and preclinical trials subjects.
S-Adenosyl-L-homocysteine hydrolase (SAHh) inhibitors have long been used as broad-range antivirals and have been recently evaluated as an experimental therapy of filovirus infections. In response to the need for a rapid laboratory testing method that could assess antiviral potency in vivo, our group developed a capillary electrophoresis (CE) method for the determination of the S-adenosyl-L-homocysteine (SAH) to S-adenosyl-L-methionine (SAM) ratio. After chloroacetaldehyde derivatization, SAH and SAM were detected using laser-induced fluorescence detection with a HeCd laser. Separation and quantitation of both SAH and SAM in human plasma were achieved in less than 1 min. The proposed method is rapid and reliable, and could be easily applied to routine monitoring of clinical and preclinical trials subjects.
S‐Adenosyl‐L‐homocysteine hydrolase (SAHh) inhibitors have long been used as broad‐range antivirals and have been recently evaluated as an experimental therapy of filovirus infections. In response to the need for a rapid laboratory testing method that could assess antiviral potency in vivo, our group developed a capillary electrophoresis (CE) method for the determination of the S‐adenosyl‐L‐homocysteine (SAH) to S‐adenosyl‐L‐methionine (SAM) ratio. After chloroacetaldehyde derivatization, SAH and SAM were detected using laser‐induced fluorescence detection with a HeCd laser. Separation and quantitation of both SAH and SAM in human plasma were achieved in less than 1 min. The proposed method is rapid and reliable, and could be easily applied to routine monitoring of clinical and preclinical trials subjects.
S ‐Adenosyl‐ L ‐homocysteine hydrolase (SAHh) inhibitors have long been used as broad‐range antivirals and have been recently evaluated as an experimental therapy of filovirus infections. In response to the need for a rapid laboratory testing method that could assess antiviral potency in vivo , our group developed a capillary electrophoresis (CE) method for the determination of the S ‐adenosyl‐ L ‐homocysteine (SAH) to S ‐adenosyl‐ L ‐methionine (SAM) ratio. After chloroacetaldehyde derivatization, SAH and SAM were detected using laser‐induced fluorescence detection with a HeCd laser. Separation and quantitation of both SAH and SAM in human plasma were achieved in less than 1 min. The proposed method is rapid and reliable, and could be easily applied to routine monitoring of clinical and preclinical trials subjects.
S-Adenosyl-L-homocysteine hydrolase (SAHh) inhibitors have long been used as broad-range antivirals and have been recently evaluated as an experimental therapy of filovirus infections. In response to the need for a rapid laboratory testing method thatcould assess antiviral potency in vivo, our group developed a capillary electrophoresis (CE) method for the determination of the S-adenosyl-L-homocysteine (SAH) to S-adenosyl-L-methionine (SAM) ratio. After chloroacetaldehyde derivatization, SAH and SAM were detected using laser-induced fluorescence detection with a HeCd laser. Separation and quantitation of both SAH and SAM in human plasma were achieved in less than 1min. The proposed method is rapid and reliable, and could be easily applied to routine monitoring of clinical and preclinical trials subjects.
Author Sbrana, Elena
Spinetti, Maria C.
Raspi, Giorgio
Bramanti, Emilia
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  organization: University Of Texas Medical Branch, Department of Pathology, Galveston, TX, USA
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  givenname: Giorgio
  surname: Raspi
  fullname: Raspi, Giorgio
  organization: Department of Chemistry, University of Pisa, Pisa, Italy
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– reference: De Clercq, E., Biochem. Parmacol. 1987, 36, 2567-2575.
– reference: Le Guenno, B., Galabru, J., Bull. Inst. Pasteur 1997, 95, 73-83.
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Snippet S‐Adenosyl‐L‐homocysteine hydrolase (SAHh) inhibitors have long been used as broad‐range antivirals and have been recently evaluated as an experimental therapy...
S ‐Adenosyl‐ L ‐homocysteine hydrolase (SAHh) inhibitors have long been used as broad‐range antivirals and have been recently evaluated as an experimental...
S-Adenosyl-L-homocysteine hydrolase (SAHh) inhibitors have long been used as broad-range antivirals and have been recently evaluated as an experimental therapy...
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SubjectTerms Acetaldehyde - analogs & derivatives
Acetaldehyde - chemistry
Adenosine analogs
Antiviral Agents - pharmacology
Antiviral drugs
Ebola
Electrophoresis, Capillary
Filovirus
Humans
S-Adenosyl-L-homocysteine hydrolase
S-Adenosylhomocysteine - analysis
S-Adenosylhomocysteine - blood
S-Adenosylmethionine - analysis
S-Adenosylmethionine - blood
Title S-Adenosyl methionine/S-adenosyl-L-homocysteine ratio determination by capillary electrophoresis employed as a monitoring tool for the antiviral effectiveness of adenosine analogs
URI https://api.istex.fr/ark:/67375/WNG-M9P58ZWG-W/fulltext.pdf
https://onlinelibrary.wiley.com/doi/abs/10.1002%2Felps.200305851
https://www.ncbi.nlm.nih.gov/pubmed/15188235
https://www.proquest.com/docview/19882207
https://www.proquest.com/docview/72007678
Volume 25
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