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2-氯-4-硝基苯基β-麦芽五糖苷的减法修饰合成及其在人α-淀粉酶差异测定中的应用。

Syntheses of subtractively modified 2-chloro-4-nitrophenyl beta-maltopentaosides and their application to the differential assay of human alpha-amylases.

作者信息

Tokutake S, Oguma T, Tobe K, Kotani K, Saito K, Yamaji N

机构信息

Research and Development Division, Kikkoman Corporation, Chiba, Japan.

出版信息

Carbohydr Res. 1993 Jan 15;238:193-213. doi: 10.1016/0008-6215(93)87013-i.

DOI:10.1016/0008-6215(93)87013-i
PMID:8431933
Abstract

Three novel maltopentaosides, 2-chloro-4-nitrophenyl O-(6-deoxy-alpha-D-xylo-hex-5-enopyranosyl)-(1-->4)-tris[O-alpha-D - glucopyranosyl-(1-->4)]-beta-D-glucopyranoside (3), 2-chloro-4-nitrophenyl O-(6-deoxy-alpha-D-glucopyranosyl)-(1-->4)-tris[O- alpha-D-glucopyranosyl-(1-->4)]-beta-D-glucopyranoside (10), and 2-chloro-4-nitrophenyl O-(3,6-anhydro-alpha-D-glucopyranosyl)-(1-->4)-tris[O-alpha-D-glucopyran osyl- (1-->4)]-beta-D-glucopyranoside (26) were synthesized by chemical and enzymatic reactions. Two human alpha-amylases, salivary alpha-amylase (HSA) and pancreatic alpha-amylase (HPA), hydrolyzed 3 and 10 with the same specificity, almost entirely at a single D-glucosidic linkage, but had no hydrolytic activity for 26. Compound 3 was hydrolyzed by each of these amylases at an approximately equal rate, while 10 was hydrolyzed by HSA 4-fold faster than by HPA. Taking advantage of the difference in the hydrolytic rate of 10, we developed a new method for the differential assay of these two human alpha-amylases.

摘要

通过化学和酶促反应合成了三种新型麦芽五糖苷,即2-氯-4-硝基苯基O-(6-脱氧-α-D-木糖己-5-烯吡喃糖基)-(1→4)-三[O-α-D-吡喃葡萄糖基-(1→4)]-β-D-吡喃葡萄糖苷(3)、2-氯-4-硝基苯基O-(6-脱氧-α-D-吡喃葡萄糖基)-(1→4)-三[O-α-D-吡喃葡萄糖基-(1→4)]-β-D-吡喃葡萄糖苷(10)和2-氯-4-硝基苯基O-(3,6-脱水-α-D-吡喃葡萄糖基)-(1→4)-三[O-α-D-吡喃葡萄糖基-(1→4)]-β-D-吡喃葡萄糖苷(26)。两种人α-淀粉酶,唾液α-淀粉酶(HSA)和胰腺α-淀粉酶(HPA),以相同的特异性水解3和10,几乎完全在单个D-糖苷键处水解,但对26没有水解活性。化合物3被这些淀粉酶中的每一种以大致相同的速率水解,而10被HSA水解的速度比被HPA快4倍。利用10水解速率的差异,我们开发了一种用于这两种人α-淀粉酶差异测定的新方法。

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