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

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

研究成果: ジャーナルへの寄稿学術誌査読

6 被引用数 (Scopus)

抄録

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.

本文言語英語
ページ(範囲)585-592
ページ数8
ジャーナルBiochemistry International
25
3
出版ステータス出版済み - 12月 1 1991
外部発表はい

!!!All Science Journal Classification (ASJC) codes

  • 生化学

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