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Conversion of murein to non-reducing fragments by enzymes from phage λ and Vi II lysates

Authors
Journal
Biochimica et Biophysica Acta (BBA) - Protein Structure
0005-2795
Publisher
Elsevier
Publication Date
Volume
342
Issue
1
Identifiers
DOI: 10.1016/0005-2795(74)90114-7
Disciplines
  • Biology

Abstract

Abstract A preparation of 200-fold purified endopeptidase from phage λ or Vi II lysates contains an enzyme which splits the amino sugar chains of murein into diffusible, but non-reducing products. The main product is a muropeptide CA with the peptide part identical with that of muropeptide C6. The results of borohydride reduction, negative Morgan-Elson test, and resistance to snail N-acetyl- β-glucosaminidase action suggest that amino sugars may be linked by a 1-1 glucosidic bond, though another structure of the amino sugar part of muropeptide CA is not escluded.

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