Biochemical Characterization and Mass Spectrometric Disulfide Bond Mapping of Periplasmic α-Amylase MalS of Escherichia coli

This publication has 60 references indexed in Scilit:

• Characterization of disulfide linkages and disulfide bond scrambling in recombinant human macrophage colony stimulating factor by fast-atom bombardment mass spectrometry of enzymatic digests
  Journal of the American Society for Mass Spectrometry, 1995
• Disulphide-coupled protein folding pathways
  Philosophical Transactions Of The Royal Society B-Biological Sciences, 1995
• Building bridges: disulphide bond formation in the cell
  Molecular Microbiology, 1994
• Disulfide linkages in the in vitro refolded intermediates of recombinant human macrophage-colony-stimulating factor: analysis of the sulfhydryl alkylation of free cysteine residues by fast-atom bombardment mass spectrometry.
  Proceedings of the National Academy of Sciences, 1994
• Protein engineering in the ?-amylase family: catalytic mechanism, substrate specificity, and stability
  Plant Molecular Biology, 1994
• The bonds that tie: Catalyzed disulfide bond formation
  Cell, 1993
• Assignment of the inter- and intramolecular disulfide linkages in recombinant human macrophage colony stimulating factor using fast atom bombardment mass spectrometry
  Biochemistry, 1993
• Molecular characterization of the MalT-dependent periplasmic alpha-amylase of Escherichia coli encoded by malS.
  Published by Elsevier ,1992
• La maltodextrine phosphorylase d' Escherichia coli
  European Journal of Biochemistry, 1967
• The characterization of the pathway of maltose utilization by Escherichia coli II. General properties and mechanism of action of amylomaltase
  Biochimica et Biophysica Acta, 1960