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NCRR's Division of Biomedical Technology supports research to develop innovative technologies and helps make them accessible to the biomedical research community.

NCRR's Division of Biomedical Technology supports research to develop innovative technologies and helps make them accessible to the biomedical research community.

NCRR's Division of Biomedical Technology supports research to develop innovative technologies and helps make them accessible to the biomedical research community.

NCRR's Division of Biomedical Technology supports research to develop innovative technologies and helps make them accessible to the biomedical research community.

NCRR's Division of Biomedical Technology supports research to develop innovative technologies and helps make them accessible to the biomedical research community.

Mass Spectrometry Resource for Biology and Medicine

Mass Spectrometry Resource for Biology and Medicine

Boston University School of Medicine
Departments of Biochemistry and Biophysics
670 Albany Street, Room 511
Boston, MA 02118-2646
www.bumc.bu.edu/msrexternal link, opens in new window

Grant No. P41 RR010888

Principal Investigator and Contact
Catherine E. Costello, Ph.D.
617-638-6490; Fax: 617-638-6491

Coprincipal Investigator
Joseph Zaia, Ph.D.
617-638-6762; Fax: 617-638-6761

Research Emphasis

The resource's mission is to conduct high-sensitivity structural determinations and analyses of biological compounds via mass spectrometry (MS). The emphasis is on glycoconjugates, oligosaccharides, and proteins; structure-activity studies related to immunology, carcinogenesis, developmental biology, parasitology, and infectious diseases; biophysical properties of carbohydrates and glycoconjugates; carbohydrate and amino acid sequence determinations of glycoproteins and proteins; and structure elucidation of unusual residues and posttranslational modifications.

Current Research

Electrospray ionization (ESI) and matrix-assisted laser desorption ionization (MALDI) methods for high-sensitivity structural determinations. Chromatographic and electrophoretic methods for analysis of complex mixtures. Derivatization and degradation protocols (low/sub pmol) with an emphasis on maximizing the MS structural information. Ion chemistry studies to improve sensitivity and elucidate fragmentation patterns of native and derivatized biopolymers. MALDI methods for surface analysis. Fourier transform ion cyclotron resonance (FT-ICR) MS in biological studies. Atomic force microscopy to complement MS studies.

Resource Capabilities

Instruments

ThermoQuest GC-Qplus GC/MS. VG/Fisons Quattro II triple quadrupole tandem MS with HPLC, Z-spray, and atmospheric pressure chemical ionization; may be operated in MS or MS/MS modes. Two Sciex/Applied Biosystems Q-Star quadrupole orthogonal acceleration time-of-flight (TOF) mass spectrometers with MALDI and ESI sources, capHPLC. Bruker Reflex IV and Finnigan MAT Vision 2000 MALDI reflectron TOF MS with nitrogen (ultraviolet, 337 nm) and Er:YAG (infrared, 2.94 mm) lasers operated in linear, reflectron, and postsource decay modes to yield molecular weight information and structural details. Two IonSpec Ultima FT-ICR mass spectrometers with external MALDI and ESI sources, 7 T active-shielded magnets, MSn capabilities with selected ion decomposition by SORI-CID, infrared multiphoton dissociation and electron capture dissociation (ECD), and high-resolution accurate mass measurements.

Special Features

Guidance on sample preparation and data interpretation. By special arrangement: microscale derivatizations and chemical and enzymatic degradations. FT-ICR MS research focuses on carbohydrate sequencing strategies; high-pressure MALDI, ECD, and software development for instrument control; and data interpretation.

National Center for Research Resources • 6701 Democracy Boulevard MSC 4874 • Bethesda MD 20892-4874 • 301-435-0888
 
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