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RECORD NUMBER: 19 OF 30

OLS Field Name OLS Field Data
Main Title Mass spectrometry of proteins and peptides /
Other Authors
Author Title of a Work
Chapman, J. R.
Publisher Humana Press,
Year Published 2000
OCLC Number 42049239
ISBN 089603609X; 9780896036093; 0896036324; 9780896036321
Subjects Proteins--Analysis. ; Peptides--Analysis. ; Amino acid sequence. ; Mass spectrometry. ; Massaspectrometrie. ; Eiwitten. ; Peptiden. ; Sequenties. ; Wetenschappelijke technieken. ; Peptides--Analyse. ; Protéines--Analyse. ; Spectroscopie de masse. ; Séquence des acides aminš. ; Massenspektrometrie ; Methode ; Proteine ; Mass Spectrometry--methods. ; Proteins--analysis--Laboratory Manuals ; Peptides--analysis--Laboratory Manuals ; Spectrum Analysis, Mass--methods--Laboratory Manuals ; Proteines--Analyse ; Sequence des acides amines ; Spectrometrie de masse
Internet Access
Description Access URL
Publisher description http://catdir.loc.gov/catdir/enhancements/fy0825/99041621-d.html
https://link.springer.com/book/10.1385/1592590454
http://www.springerprotocols.com/BookToc/doi/10.1385/1592590454
Holdings
Library Call Number Additional Info Location Last
Modified
Checkout
Status
EKCM  QP551.M33 2000 NHEERL/GED Library/Gulf Breeze,FL 03/04/2005
Collation xiv, 538 pages : illustrations ; 24 cm.
Notes
Includes bibliographical references and index.
Contents Notes
De Novo peptide sequencing by nanoelecrospray tandem mass spectrometry using triple quadrupole and quadrupole/time-of-flight instruments -- Direct analysis of proteins in mixtures: application to protein complexes -- Characterizaton of a mutant recombinant S100 protein using electrospray ionization mass spectrometry -- Searching sequence databases via De Novo peptide sequencing by tandem mass spectrometry -- Signature peptides: from analytical chemistry to functional genomics -- Ivestigating the higher order structure of proteins: hydrogen exchange, proteolytic fragmentation, and mass spectrometry -- Probing protein surface topology by chemical surface labeling, crosslinking, and mass spectrometry -- Secondary structure of peptide ions in the gas phase evaluated by MIKE spectrometry: relevance to native conformations -- Preparation and mass spectrometric analysis of S-nitrosohemoglobin -- Multiple and subsequent MALDI-MS on-target chemical reactions for the characterization of dislfide bonds and primary structures of proteins -- Epitope mapping by a combination of epitope excision and MALDI-MS -- Identification of active site residues in glycosidases by use of tandem mass spectrometry -- Probing protein-protein interactions with mass spectrometry -- Studies of noncovalent complexes in an electrospray ionization/time-of-flight mass spectrometer -- Kinetic analysis of enzymatic and nonenzymatic degradation of peptides by MALDI-TOFMS -- Characterization of protein glycosylation by MALDI-TOFMS -- Positive and negative labeling of human proinsulin, insulin and C-peptide with stable isotopes: new tools for in vivo pharmacokinetic and metabolic studies -- Identification of snake species by toxin mass fingerprinting of their venoms -- Mass spectrometric characterization of the [beta]-subunit of human chorionic gonadotropin -- Analysis of gluten in foods by MALD-TOFMS -- Quantitation of nucleotidyl cyclase and cyclic nucleotide-sensitive protein kinase activities by fast-atom bombardment mass spectrometry: a paradigm for multiple component monitoring in enzyme incubations by quantitative mass spectrometry -- Influence of salts, buffers, detergents, solvents, and matrices on MALDI-MS protein analysis in complex mixtures -- Sample preparation techniques for peptides and proteins analyzed by MALDI-MS -- Analysis of hydrophobic proteins and peptides by mass spectrometry -- Analysis of proteins and peptides directly from biological fluids by immunoprecipitation/mass spectrometry -- Detection of molecular determinants in complex biological systems using MALDI-TOF affinity mass spectrometry -- Rapid identification of bacteria based on spectral patterns using MALDI-TOFMS -- Appendices.