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 language | English (US) |
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Title of host publication | Proceedings 50th ASMS Conference on Mass Spectrometry and Allied Topics |
Pages | 269-270 |
Number of pages | 2 |
State | Published - 2002 |
Event | Proceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics - Orlando, FL, United States Duration: Jun 2 2002 → Jun 6 2002 |
Other
Other | Proceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics |
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Country/Territory | United States |
City | Orlando, FL |
Period | 6/2/02 → 6/6/02 |
ASJC Scopus subject areas
- Spectroscopy