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Action ofendo-α- N - acetylgalactosaminidasefromAlcaligenessp. on amino acid-O-glycans: Comparison with the enzyme fromDiplococcus pneumoniae

Authors
Journal
Biochemical and Biophysical Research Communications
0006-291X
Publisher
Elsevier
Publication Date
Volume
169
Issue
2
Identifiers
DOI: 10.1016/0006-291x(90)90395-4
Disciplines
  • Biology

Abstract

Abstract Endo-α- N-acetylgalactosaminidase from Alcaligenes sp. released the disaccharide, Galβ1→3GalNAc, from both dansylated serine-GalNAc-Gal and threonine-GalNAc-Gal, and showed higher activity on the former than the latter. The Km values were 0.17 mM and 1.43 mM with DNS-Ser-GalNAc-Gal and DNS-Thr-GalNAc-Gal, respectively. The optimum pHs were found to be 4.5–7.5 and 4.5–6.0 on DNS-Ser-GalNAc-Gal and DNS-Thr-GalNAc-Gal, respectively. On the contrary, the enzyme from Diplococcus pneumoniae had low activity to release the disaccharide from the amino acid- O-glycans. The possibility that the same O-glycoside but linked to different aglycon amino acids may play a different biological role in glycoproteins is discussed.

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