Purification and characterization of α-N-acetylgalactosaminidases 1 and 2 from the starfish Asterina amurensis

• Harun-Or-RASHID Md.

  Department of Health Chemistry, Faculty of Pharmaceutical Sciences, Niigata University of Pharmacy and Applied Life Sciences

• MATSUZAWA Tomomi

  Department of Health Chemistry, Faculty of Pharmaceutical Sciences, Niigata University of Pharmacy and Applied Life Sciences

• SATOH Youichi

  Department of Health Chemistry, Faculty of Pharmaceutical Sciences, Niigata University of Pharmacy and Applied Life Sciences

• SHIRAISHI Takayuki

  Laboratory of Health Chemistry, Nihon Pharmaceutical University

• ANDO Masayuki

  Department of Health Chemistry, Faculty of Pharmaceutical Sciences, Niigata University of Pharmacy and Applied Life Sciences

• SADIK Golam

  Department of Health Chemistry, Faculty of Pharmaceutical Sciences, Niigata University of Pharmacy and Applied Life Sciences

• UDA Yutaka

  Department of Health Chemistry, Faculty of Pharmaceutical Sciences, Niigata University of Pharmacy and Applied Life Sciences

書誌事項

タイトル別名

• Purification and Characterization of .ALPHA.-N-Acetylgalactosaminidases I and II from the Starfish Asterina amurensis
• Purification and characterization of a N acetylgalactosaminidases 1 and 2 from the starfish Asterina amurensis
• Purification and Characterization of α-<i>N</i>-Acetylgalactosaminidases I and II from the Starfish<i>Asterina amurensis</i>

抄録

Two α-N-acetylgalactosaminidases, α-N-acetylgalactosaminidase (α-GalNAcase) I and II, were purified from the digestive organ of starfish. Purified α-GalNAcase I and II gave nearly single protein bands on SDS-polyacrylamide gel electrophoresis, individually. Even the final preparation of α-GalNAcase I contained α-galactosidase activity, while α-GalNAcase II was almost free from that activity with p-nitrophenyl and 4-methylumbelliferyl α-N-acetylgalactosaminides as substrates. α-GalNAcase I and II both hydrolyzed terminal α-N-acetylgalactosaminyl linkages of the natural compounds investigated: Forssman hapten glycolipid, blood group A active oligosaccharide and GalNAc-α1-O-serine. On the other hand, oligosaccharides, and glycolipid containing α-galactosyl terminals were hydrolyzed by α-GalNAcase I but not by α-GalNAcase II. The substrate specificities and other enzymatic properties of α-GalNAcase I were similar to those of human placental α-GalNAcase, but distinct from α-GalNAcase II.

収録刊行物

• Ｂｉｏｓｃｉｅｎｃｅ，　Ｂｉｏｔｅｃｈｎｏｌｏｇｙ，　ａｎｄ　Ｂｉｏｃｈｅｍｉｓｔｒｙ

  Ｂｉｏｓｃｉｅｎｃｅ，　Ｂｉｏｔｅｃｈｎｏｌｏｇｙ，　ａｎｄ　Ｂｉｏｃｈｅｍｉｓｔｒｙ 74 (2), 256-261, 2010

  公益社団法人 日本農芸化学会

キーワード

• α-<I>N</I>-acetylgalactosaminidase
• α-galactosidase
• substrate specificity
• starfish

詳細情報

• CRID: 1390282681453635968
• NII論文ID: 10027551089
• NII書誌ID: AA10824164
• DOI: 10.1271/bbb.90178
• ISSN: 13476947
• ISSN: 09168451
• NDL書誌ID: 10579817
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I10579817
• Web Site: http://www.tandfonline.com/doi/pdf/10.1271/bbb.90178
• 本文言語コード: en
• データソース種別:
  • JaLC
  • NDL
  • Crossref
  • CiNii Articles
• 抄録ライセンスフラグ: 使用不可