Primary sequence information from intact proteins by electrospray ionization tandem mass spectrometry

Journal Article · Fri Apr 13 00:00:00 EDT 1990 · Science (Washington, D.C.); (USA)

DOI:https://doi.org/10.1126/science.2326633· OSTI ID:6511533

Loo, J A; Edmonds, C G; Smith, R D ^[1]

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1. Pacific Northwest Laboratory, Richland, WA (USA)

Tandem mass spectrometry has been used to obtain information related to portions of the primary sequence for an intact protein, bovine ribonuclease A. Multiply charged molecular ions, generated by electrospray ionization, were collisionally dissociated at low energies in a triple quadrupole mass spectrometer to yield singly and multiply charged fragment ions that can be assigned to the known sequence of the protein. Dissociation of the highly charged molecular ions resulted in pairs of complementary product ions. The higher order (gas-phase) protein structure affects the dissociation processes, as observed in comparisons of tandem mass spectra of the native and disulfide-reduced forms of ribonuclease A. 22 refs., 4 figs.

• DOE Contract Number: AC06-76RL01830
• OSTI ID: 6511533
• Journal Information: Science (Washington, D.C.); (USA), Journal Name: Science (Washington, D.C.); (USA) Vol. 201-204:248; ISSN SCIEA; ISSN 0036-8075
• Country of Publication: United States
• Language: English

Related Subjects

37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY
400201 -- Chemical & Physicochemical Properties
550300* -- Cytology
59 BASIC BIOLOGICAL SCIENCES
ANIMALS
CATTLE
DATA
DOMESTIC ANIMALS
ENZYMES
ESTERASES
EXPERIMENTAL DATA
HYDROLASES
INFORMATION
IONIZATION
MAMMALS
MASS SPECTRA
MOLECULAR STRUCTURE
NUMERICAL DATA
PHOSPHODIESTERASES
RNA-ASE
RUMINANTS
SPECTRA
VERTEBRATES