Mass spectrometric investigations on higher molecular weight toxins and antibodies. Final report, February-March 1995
The mass spectrometric techniques were effectively applied for the ultra-sensitive detection of individual toxins or venom components as well as to deduce their primary structures. Numerous proteinaceous toxins with assorted toxicities originating from several sources have been ionized under electrospray (ESI), matrix assisted laser desorption (MALDI) and continuous flow-fast atom bombardment (frit-FAB) ionization conditions and detected by mass spectrometric (MS) methods to measure their corresponding molecular masses. The primary structures or the amino acid sequences of a small peptide (<3,500 Da) can be deduced by subjecting its protonated molecular ions to collisionally induced dissociations and detecting the corresponding product (daughter) ions. The process is termed as tandem mass spectrometric analysis (MS/MS). Simple chemical and enzymatic modifications of a larger polypeptide or protein, in addition to MS/MS procedures, are required to characterize their primary structures. The measured sensitivities under both approaches ranged from 0.2 to 2 picomoles of the intact peptides. Similarly, the molecular masses of some commercial antibodies were also determined using only 0.5-1.0 picomole amounts.
- Research Organization:
- Edgewood Research, Development and Engineering Center, Aberdeen Proving Ground, MD (United States)
- OSTI ID:
- 381602
- Report Number(s):
- AD-A--310534/3/XAB; ERDEC-TR--323
- Country of Publication:
- United States
- Language:
- English
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