Differential Assay of Human Pancreatic and Salivary α-Amylases with p-Nitrophenyl 6^5-O-β-D-Galacopyraosyl-α-maltopentaoside as the Substrate
スポンサーリンク
概要
- 論文の詳細を見る
p-Nitrophenyl 6^5-O-β-D-galactopyraosyl-α-maltopentaoside (L^6G5P) was synthesized by the sequential use of the transglycosylation and hydrolytic action of β-D-galactosidase from Bacillus circulans. The enzyme produced L^6G5P (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 L^6G5P was calculated by analysis of the digests by high-pressure liquid chromatography. The modes of action of the two isozymes differed. Both hydrolyzed L^6G5P 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, L^6G5P could be used to assay of the two enzymes differentially in serum.
- 社団法人日本農芸化学会の論文
- 1992-12-23
著者
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Ogawa Koichi
Department Of Applied Informatics Faculty Of Science And Engineering Hosei University
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Usui T
Department Of Appied Biological Chemistry Faculty Of Agriculture Shizuoka University
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Usui Taichi
Department Of Agricultural Chemistry Faculty Of Agriculture Shizuoka University
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MATSUI Hidenori
Department of Infectious Disease and Immunology, The Kitasato Institute
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Ogawa K
Department Of Food Science For Health Faculty Of Health And Nutrition Minami Kyushu University
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Ogawa Koichi
Department Of Anatomy Fukuoka University School Of Medicine
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Matsui Hidenori
Department Of Appied Biological Chemistry Faculty Of Agriculture Shizuoka University
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Ogawa K
Iwaki Meisei Univ. Iwaki Jpn
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Ogawa Koichi
Department Of Anatomy Fukuoka University School Of Medicinde
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MATSUI Hidenori
Department of Agricultural Chemistry, Faculty of Agriculture, Shizuoka University
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