Localization of anO-glycosylated site in the recombinant barley α-amylase 1 produced in yeast and correction of the amino acid sequence using matrix-assisted laser desorption/ionization mass spectrometry of peptide mixtures
Author:
Publisher
Wiley
Subject
Molecular Medicine,Biochemistry,Spectroscopy
Reference38 articles.
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1. The activity of barley α-amylase on starch granules is enhanced by fusion of a starch binding domain from Aspergillus niger glucoamylase;Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics;2006-02
2. Tyrosine 105 and Threonine 212 at Outermost Substrate Binding Subsites –6 and +4 Control Substrate Specificity, Oligosaccharide Cleavage Patterns, and Multiple Binding Modes of Barley α-Amylase 1;Journal of Biological Chemistry;2004-03
3. Identification of 2D-gel proteins: A comparison of MALDI/TOF peptide mass mapping to μ LC-ESI tandem mass spectrometry;Journal of the American Society for Mass Spectrometry;2003-09-01
4. MALDI-TOF mass spectrometry in protein chemistry;Proteomics in Functional Genomics;2000
5. Matrix-assisted laser desorption/ionization mass spectrometry of carbohydrates;MASS SPECTROM REV;1999
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