Determination of glycosylation sites using a protein sequencer and deglycosylation of native yeast invertase by endo-β-N-acetylglucosaminidase

Kaoru Takegawa, M. Yoshikawa, T. Mishima, M. Nakoshi, S. Iwahara

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

Endo-β-N-acetylglucosaminidase from Arthrobacter protophormiae was tested for its capacity to release N-linked sugar chains from native yeast invertase. The enzyme liberated about 80% of the sugar chains from the native invertase. Deglycosylated invertase was digested by chymotrypsin or pepsin, and twelve N-acetylglucosamine-containing glycopeptides were isolated. The amino acid sequences of these glycopeptides were analyzed by a protein sequencer, and the elution position of 4-L-aspartylglycosylamine was directly identified by conventional sequencing. The endo-β-N-acetylglucosaminidase was found to remove mainly nine sugar chains from native invertase.

Original languageEnglish
Pages (from-to)585-592
Number of pages8
JournalBiochemistry International
Volume25
Issue number3
Publication statusPublished - 1991
Externally publishedYes

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Glycosylation
beta-Fructofuranosidase
Acetylglucosaminidase
Yeast
Yeasts
Sugars
Glycopeptides
Proteins
Arthrobacter
Acetylglucosamine
Pepsin A
Chymotrypsin
Amino Acid Sequence
Amino Acids
endo-alpha-sialidase
Enzymes

All Science Journal Classification (ASJC) codes

  • Biochemistry

Cite this

Determination of glycosylation sites using a protein sequencer and deglycosylation of native yeast invertase by endo-β-N-acetylglucosaminidase. / Takegawa, Kaoru; Yoshikawa, M.; Mishima, T.; Nakoshi, M.; Iwahara, S.

In: Biochemistry International, Vol. 25, No. 3, 1991, p. 585-592.

Research output: Contribution to journalArticle

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