Differential Assay of Human Pancreatic and Salivary<i>α</i>-Amylases with<i>p</i>-Nitrophenyl 6⁵-<i>O</i>-<i>β</i>-<scp>D</scp>-Galacopyraosyl-<i>α</i>-maltopentaoside as the Substrate

• OGAWA Koichi

• MATSUI Hidenori

• USUI Taichi

書誌事項

タイトル別名

• Differential Assay of Human Pancreatic and Salivary .ALPHA.-Amylases with p-Nitrophenyl 65-O-.BETA.-D-Galacopyraosyl-.ALPHA.-maltopentaoside as the Substrate.

抄録

p-Nitrophenyl 6⁵-O-β-D-galactopyraosyl-α-maltopentaoside (L⁶G5P) was synthesized by the sequential use of the transglycosylation and hydrolytic action of β-D-galactosidase from Bacillus circulans. The enzyme produced L⁶G5P (at a yield of 8.0% based on the amount of p-nitrophenyl α-maltopentaoside added) from lactose as the donor and p-nitrophenyl α-maltopentaoside as the acceptor. The frequency at which of human pancreatic α-amylase and salivary α-amylase catalyzed the cleavage of glycosidic linkages in L⁶G5P was calculated by analysis of the digests by high-pressure liquid chromatography. The modes of action of the two isozymes differed. Both hydrolyzed L⁶G5P and produced p-nitrophenyl α-maltoside and p-nitrophenyl α-D-glucopyranoside, but human pancreatic α-amylase produced more of the latter than human salivary α-amylase. Thus, L⁶G5P could be used to assay of the two enzymes differentially in serum.

収録刊行物

• Ｂｉｏｓｃｉｅｎｃｅ，　Ｂｉｏｔｅｃｈｎｏｌｏｇｙ，　ａｎｄ　Ｂｉｏｃｈｅｍｉｓｔｒｙ

  Ｂｉｏｓｃｉｅｎｃｅ，　Ｂｉｏｔｅｃｈｎｏｌｏｇｙ，　ａｎｄ　Ｂｉｏｃｈｅｍｉｓｔｒｙ 56 (12), 1933-1936, 1992

  公益社団法人 日本農芸化学会

キーワード

• Organic Chemistry
• Molecular Biology
• Applied Microbiology and Biotechnology
• General Medicine
• Biochemistry
• Analytical Chemistry
• Biotechnology

詳細情報

• CRID: 1390001206470148096
• NII論文ID: 110002691707
• NII書誌ID: AA10824164
• DOI: 10.1271/bbb.56.1933
• COI: 1:CAS:528:DyaK3sXitVyjur8%3D
• ISSN: 13476947
• ISSN: 09168451
• Web Site: http://www.tandfonline.com/doi/pdf/10.1271/bbb.56.1933
• 本文言語コード: en
• データソース種別:
  • JaLC
  • Crossref
  • CiNii Articles
• 抄録ライセンスフラグ: 使用不可