Abstract

Fourier transform mass spectrometry (FTMS) is a rapidly developing new instrument concept with possible important application to biomolecule research, especially large non-volatile molecule. The objectives of this program are to develop a Cs+ desorption ionization source adaptable to FTMS and pursue the development of high mass FTMS with specific emphasis on biomolecules. In this proposal the unique aspects of FTMS for biomolecule studies, i.e., high sensitivity/high resolution, are discussed and specific examples of preliminary studies are presented. The continued development of biomolecule FTMS is presented with particular emphasis on high mass molecules (greater than m/z 1,000) using Cs+ desorption ionization. The model systems proposed for extensive study include vitamins (vitamin B12 and vitamin B12 coenzyme), antibiotics (avoparcin and adenomycen, etc.), peptides (melittin and glucagon), and bovine insulin. These molecules span the mass range m/z 1,000 - m/z 5,000 and the present available mass range of FTMS. Also, these molecules represent suitable challenges to provide a critical accessment of FTMS for the analysis of biomolecules.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
1R01GM033780-01
Application #
3283780
Study Section
Metallobiochemistry Study Section (BMT)
Project Start
1984-12-01
Project End
1987-11-30
Budget Start
1984-12-01
Budget End
1985-11-30
Support Year
1
Fiscal Year
1985
Total Cost
Indirect Cost

  Institution

Name
Texas A&M University
Department
Type
Schools of Arts and Sciences
DUNS #
City
College Station
State
TX
Country
United States
Zip Code
77845

  Publications

Preston, L M; Murray, K K; Russell, D H (1993) Reproducibility and quantitation of matrix-assisted laser desorption ionization mass spectrometry: effects of nitrocellulose on peptide ion yields. Biol Mass Spectrom 22:544-50
Solouki, T; Russell, D H (1992) Laser desorption studies of high mass biomolecules in Fourier-transform ion cyclotron resonance mass spectrometry. Proc Natl Acad Sci U S A 89:5701-4
Hanson, C D; Kerley, E L; Russell, D H (1989) High-resolution ion partitioning technique by phase-specific ion excitation for Fourier transform ion cyclotron resonance. Anal Chem 61:83-5
Hanson, C D; Castro, M E; Russel, D H (1989) Phase synchronization of an ion ensemble by frequency sweep excitation in Fourier transform ion cyclotron resonance. Anal Chem 61:2130-6
Hanson, C D; Kerley, E L; Castro, M E et al. (1989) Ion detection by Fourier transform ion cyclotron resonance: the effect of initial radial velocity on the coherent ion packet. Anal Chem 61:2040-6
Russell, D H; McGlohon, E S; Mallis, L M (1988) Fast-atom bombardment tandem mass spectrometry studies of organo-alkali-metal ions of small peptides. Competitive interaction of sodium with basic amino acid substituents. Anal Chem 60:1818-24
Mallis, L M; Raushel, F M; Russell, D H (1987) Differentiation of isotopically labeled nucleotides using fast atom bombardment tandem mass spectrometry. Anal Chem 59:980-4
Amster, I J; McLafferty, F W; Castro, M E et al. (1986) Detection of mass 16 241 ions by Fourier-transform mass spectrometry. Anal Chem 58:483-5
Mallis, L M; Russell, D H (1986) Fast atom bombardment--tandem mass spectrometry studies of organo-alkali metal ions of small peptides. Anal Chem 58:1076-80
Hilscher, L W; Hanson, C D; Russell, D H et al. (1985) Measurement of positional isotope exchange rates in enzyme-catalyzed reactions by fast atom bombardment mass spectrometry: application to argininosuccinate synthetase. Biochemistry 24:5888-93

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