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Isolation of two endo-beta-N-acetylglucosaminidases with different specificities from Pseudomonas sp.
- Source :
-
Biochemistry international [Biochem Int] 1991 Jul; Vol. 24 (5), pp. 793-9. - Publication Year :
- 1991
-
Abstract
- Two endo-beta-N-acetylglucosaminidases (PI and PII) have been isolated from the culture fluid of Pseudomonas sp. The substrate specificity of the PI enzyme was very similar to that of Endo-H from Streptomyces plicatus. On the contrary, the PII enzyme had a novel substrate specificity that degraded both high-mannose type and hybrid type oligosaccharides derived from ovalbumin, and the core structure of complex type oligosaccharides derived from human transferrin and porcine pancreatic lipase.
- Subjects :
- Glycopeptides metabolism
Hexosaminidases metabolism
Hydrogen-Ion Concentration
Lipase metabolism
Mannose chemistry
Mannose metabolism
Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase metabolism
Molecular Weight
Pseudomonas chemistry
Pseudomonas immunology
Streptomyces chemistry
Streptomyces enzymology
Streptomyces immunology
Substrate Specificity
Transferrin metabolism
Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase isolation & purification
Oligosaccharides metabolism
Pseudomonas enzymology
Subjects
Details
- Language :
- English
- ISSN :
- 0158-5231
- Volume :
- 24
- Issue :
- 5
- Database :
- MEDLINE
- Journal :
- Biochemistry international
- Publication Type :
- Academic Journal
- Accession number :
- 1776950