Isolation of two endo-β-N-acetylglucosaminidases with different specificities from Pseudomonas sp

Kaoru Takegawa, T. Naitoh, S. Iwahara

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

Two endo-β-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.

Original languageEnglish
Pages (from-to)793-799
Number of pages7
JournalBiochemistry international
Volume24
Issue number5
Publication statusPublished - Dec 3 1991

Fingerprint

Acetylglucosaminidase
Substrate Specificity
Pseudomonas
Oligosaccharides
Ovalbumin
Streptomyces
Substrates
Enzymes
Transferrin
Mannose
Lipase
Swine
Fluids
endo-alpha-sialidase

All Science Journal Classification (ASJC) codes

  • Biochemistry

Cite this

Isolation of two endo-β-N-acetylglucosaminidases with different specificities from Pseudomonas sp. / Takegawa, Kaoru; Naitoh, T.; Iwahara, S.

In: Biochemistry international, Vol. 24, No. 5, 03.12.1991, p. 793-799.

Research output: Contribution to journalArticle

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