Application of electrospray mass spectrometry to the characterization of recombinant proteins up to 44 kDa
- 1 November 1990
- journal article
- Published by Wiley in Journal of Mass Spectrometry
- Vol. 19 (11) , 692-704
- https://doi.org/10.1002/bms.1200191108
Abstract
No abstract availableKeywords
This publication has 30 references indexed in Scilit:
- Isolation and structure elucidation of a novel 5‐kDa peptide from neurohaemal lobes of the corpora cardiaca of Locusta migratoria (Insecta, Orthoptera)European Journal of Biochemistry, 1990
- Isolation and structure of two novel 6‐kDa dimeric peptides from the copora cardiaca of the insect Locusta migratoriaEuropean Journal of Biochemistry, 1989
- Mass spectrometry analyses of recombinant hirudins (7 kDa)Biochemistry, 1989
- Contributions of mass spectrometry to peptide and protein structureJournal of Mass Spectrometry, 1988
- Purification and characterization of low-molecular-weight beef heart proteolipids: Use of fast atom bombardment-mass spectrometry for identificationAnalytical Biochemistry, 1988
- Primary structure of Paim I, an .alpha.-amylase inhibitor from Streptomyces corchorushii, as determined by the combination of Edman degradation and fast atom bombardment mass spectrometryBiochemistry, 1987
- The analysis of small proteins in the molecular weight range 10–24 kDa by magnetic sector mass spectrometryRapid Communications in Mass Spectrometry, 1987
- The primary structure of thioredoxin from Chromatium vinosum determined by high-performance tandem mass spectrometryBiochemistry, 1987
- Mass spectrometryAnalytical Chemistry, 1986
- FAB-MAPPING of recombinant-DNA protein productsBiochemical and Biophysical Research Communications, 1983