High throughput characterization of hemoglobin from neonates using MALDI-TOF MS

Urban A. Kiernan, Peter Williams, Randall W. Nelson

Research output: Chapter in Book/Report/Conference proceedingConference contribution

Abstract

MALDI-TOF targets were used to create a high throughput platform capable of characterizing hemoglobin from neonates at a rate of ∼ 100 samples per hour. Ninety-six neonate dried blood blot samples were collected and isolated in individual wells of a 96-well titer plate and robotically processed in parallel acidified hemoglobin solutions. The intact chains of 96 hemoglobin samples were screened. The absence of an additional signal, either split or shifted by ∼-30 Da, indicates that the mutation was present in the first eight residues of the β-chain and due to the β6Glu Val substitution.

Original languageEnglish (US)
Title of host publicationProceedings 50th ASMS Conference on Mass Spectrometry and Allied Topics
Pages269-270
Number of pages2
StatePublished - 2002
EventProceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics - Orlando, FL, United States
Duration: Jun 2 2002Jun 6 2002

Other

OtherProceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics
CountryUnited States
CityOrlando, FL
Period6/2/026/6/02

ASJC Scopus subject areas

  • Spectroscopy

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  • Cite this

    Kiernan, U. A., Williams, P., & Nelson, R. W. (2002). High throughput characterization of hemoglobin from neonates using MALDI-TOF MS. In Proceedings 50th ASMS Conference on Mass Spectrometry and Allied Topics (pp. 269-270)