Rapid Microwave-Assisted Chemical Cleavage - Mass Spectrometric Method for the Identification of Hemoglobin Variants in Blood. Alam, A., Mataj, A., Yang, Y., Yang, Y., Boysen, R. I, Bowden, D. K., Bowden, D. K., & Hearn, M. T. W. Analytical Chemistry, 82(21):8922–8930, October, 2010. MAG ID: 2037796036doi abstract bibtex A sensitive, rapid analytical method has been developed for the characterization of human hemoglobin disorders with very small volumes (\textless1 μL) of blood. As an alternative to conventional enzymatic digestion, a site-specific chemical cleavage method has been established using 0.05% formic acid under microwave-irradiation conditions for short time intervals, for example, less than 10 min. Peptide analysis was performed by MALDI TOF MS and capillary liquid chromatographic ESI MS/MS. The cleavage of the hemoglobin chains with formic acid occurred at either side or at both sides (C- and N-terminal) of aspartic acid residues, but preferentially N-terminally. The method has been applied to blood samples from hemoglobin S carrier heterozygotes and hemoglobin S thalassaemia compound heterozygotes with a reduced expression level of hemoglobin S. Both MALDI TOF MS and ESI MS/MS analysis allowed the identification of the hemoglobin S “signature” peptide. This alternative method of sample preparation is compatible wit...
@article{alam_rapid_2010,
title = {Rapid {Microwave}-{Assisted} {Chemical} {Cleavage} - {Mass} {Spectrometric} {Method} for the {Identification} of {Hemoglobin} {Variants} in {Blood}},
volume = {82},
doi = {10.1021/ac1017106},
abstract = {A sensitive, rapid analytical method has been developed for the characterization of human hemoglobin disorders with very small volumes ({\textless}1 μL) of blood. As an alternative to conventional enzymatic digestion, a site-specific chemical cleavage method has been established using 0.05\% formic acid under microwave-irradiation conditions for short time intervals, for example, less than 10 min. Peptide analysis was performed by MALDI TOF MS and capillary liquid chromatographic ESI MS/MS. The cleavage of the hemoglobin chains with formic acid occurred at either side or at both sides (C- and N-terminal) of aspartic acid residues, but preferentially N-terminally. The method has been applied to blood samples from hemoglobin S carrier heterozygotes and hemoglobin S thalassaemia compound heterozygotes with a reduced expression level of hemoglobin S. Both MALDI TOF MS and ESI MS/MS analysis allowed the identification of the hemoglobin S “signature” peptide. This alternative method of sample preparation is compatible wit...},
number = {21},
journal = {Analytical Chemistry},
author = {Alam, Asif and Mataj, Agron and Yang, Yuanzhong and Yang, Yuanzhong and Boysen, Reinhard I and Bowden, Donald K. and Bowden, D. K. and Hearn, Milton Thomas William},
month = oct,
year = {2010},
doi = {10.1021/ac1017106},
pmid = {20936783},
note = {MAG ID: 2037796036},
pages = {8922--8930},
}
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Peptide analysis was performed by MALDI TOF MS and capillary liquid chromatographic ESI MS/MS. The cleavage of the hemoglobin chains with formic acid occurred at either side or at both sides (C- and N-terminal) of aspartic acid residues, but preferentially N-terminally. The method has been applied to blood samples from hemoglobin S carrier heterozygotes and hemoglobin S thalassaemia compound heterozygotes with a reduced expression level of hemoglobin S. Both MALDI TOF MS and ESI MS/MS analysis allowed the identification of the hemoglobin S “signature” peptide. 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As an alternative to conventional enzymatic digestion, a site-specific chemical cleavage method has been established using 0.05\\% formic acid under microwave-irradiation conditions for short time intervals, for example, less than 10 min. Peptide analysis was performed by MALDI TOF MS and capillary liquid chromatographic ESI MS/MS. The cleavage of the hemoglobin chains with formic acid occurred at either side or at both sides (C- and N-terminal) of aspartic acid residues, but preferentially N-terminally. The method has been applied to blood samples from hemoglobin S carrier heterozygotes and hemoglobin S thalassaemia compound heterozygotes with a reduced expression level of hemoglobin S. Both MALDI TOF MS and ESI MS/MS analysis allowed the identification of the hemoglobin S “signature” peptide. 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