Biochemical characterization of a polysialyltransferase from Mannheimia haemolytica A2 and comparison to other bacterial polysialyltransferases

From National Research Council Canada

DOIResolve DOI: https://doi.org/10.1371/journal.pone.0069888
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Affiliation
  1. National Research Council of Canada. Human Health Therapeutics
FormatText, Article
Subjectbacterial enzyme; glycan; glycoprotein; hybrid protein; maltose binding protein; polysialic acid; polysialyltransferase; recombinant enzyme; unclassified drug; binding site; carbohydrate analysis; cell migration; cell surface; comparative study; DNA sequence; enzyme activity; enzyme analysis; enzyme kinetics; enzyme stability; enzyme synthesis; Escherichia coli; Mannheimia haemolytica; Neisseria meningitidis; neuroprogenitor cell; nucleotide sequence; pH; protein expression; protein localization; protein modification; solubility; stem cell; suicide substrate; thermostability; wound healing
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LanguageEnglish
Peer reviewedYes
NPARC number21269716
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Record identifier8e519624-1cfd-4675-bfa0-d3f56edf563d
Record created2013-12-13
Record modified2022-11-18
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