Comparative Study
doi: 10.1016/0006-291x(90)90395-4.
Action of endo-alpha-N-acetylgalactosaminidase from Alcaligenes sp. on amino acid-O-glycans: comparison with the enzyme from Diplococcus pneumoniae
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- PMID: 2357231
- DOI: 10.1016/0006-291x(90)90395-4
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Comparative Study
Action of endo-alpha-N-acetylgalactosaminidase from Alcaligenes sp. on amino acid-O-glycans: comparison with the enzyme from Diplococcus pneumoniae
Biochem Biophys Res Commun.
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Abstract
Endo-alpha-N-acetylgalactosaminidase from Alcaligenes sp. released the disaccharide, Gal beta 1----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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