The linkage of teleost skin keratan sulfate to protein

Makoto Ito, Tatsuya Yamagata

研究成果: Contribution to journalArticle査読

2 被引用数 (Scopus)

抄録

The linkage of teleost skin keratan sulfate to protein was investigated. Afeter its exhaustive digestion with pronase, peptidokeratan sulfate was obtained with aspartic acid as the predominant amino acid. The N-terminal of the amino acid residues of the preparation was dansylated, and the carbohydrate-peptide linkage fragment was isolated, with the aid of fluorescence, by sequential digestion with Flavobacterium endo-β-galactosidase, β-galactosidase, β-N-acetylhexosaminidase and endo-β-N-acetylglucosaminidase D, followed by Bio-Gel p-4 column chromatography. The structure of the dansylated fragment thus obtained was identified dansylated asparaginyl N-acetyl-D-glucosamine. Treatment of the dansylated keratan sulfate peptide with almond glycopeptidase, which specially cleaves thet asparaginyl N-acetyl-D-glucosamine linkage in the glycoproteins, also showed asparaginyl N-aceytyl-D-glucosamine linkage to be in the core region of this keratan sulfate. We conclude that teleost skin keratan sulfate is bound to protein via an N-glycosyl linkage between N-acetyl-D-glucosamine and asparagine. The keratan sulfate core apparently consist of trimannosyl-N,N′-diacetylchitobiose units, considering the specificity of endo-β-N-acetylglucosaminidase D.

本文言語英語
ページ(範囲)381-387
ページ数7
ジャーナルBBA - General Subjects
801
3
DOI
出版ステータス出版済み - 10 16 1984
外部発表はい

All Science Journal Classification (ASJC) codes

  • 生化学
  • 生物理学
  • 分子生物学

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