Comparative studies of asparagine-linked oligosaccharide structures of rat liver microsomal and lysosomal β-glucuronidases

Tsuguo Mizuochi, Yukio Nishimura, Keitaro Kato, Akira Kobata

研究成果: Contribution to journalArticle査読

25 被引用数 (Scopus)

抄録

The sugar chains of microsomal and lysosomal β-glucuronidases of rat liver were studied by endo-β-N-acetylglucosaminidase H digestion and by hydrazinolysis. Only a part of the oligosaccharides released from microsomal β-glucuronidase was an acidic component. The acidic component was not hydrolyzed by sialidase and by calf intestinal and Escherichia coli alkaline phosphatases, but was converted to a neutral component by phosphatase digestion after mild acid treatment indicating the presence of a phosphodiester group. The neutral oligosaccharide portion of microsomal enzyme was a mixture of five high mannose-type sugar chains: (Manα1 → 2)0~4 [Manα1 → 6(Manα1 → 3)Manα1 → 6(Manα1 → 3)Manβ1 → 4GlcNAcβ1 → 4GlcNAc]. In contrast, lysosomal enzyme contains only Manα1 → 6 (Manα1 → 3) Manα1 → 6(Manα1 → 3) Manβ1 → 4GlcNAcβ1 → 4GlcNAc. The result indicates that removal of α1 → 2-linked mannosyl residues from (Manα1 → 2)4[Manα1 → 6(Manα1 → 3)Manα1 → 6(Manα1 → 3)Manβ1 → 4GlcNAcβ1 → 4GlcNAc → Asn] starts already in the endoplasmic reticulum of rat liver.

本文言語英語
ページ(範囲)298-303
ページ数6
ジャーナルArchives of Biochemistry and Biophysics
209
1
DOI
出版ステータス出版済み - 6 1981

All Science Journal Classification (ASJC) codes

  • 生物理学
  • 生化学
  • 分子生物学

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