Syntheses of subtractively modified 2-chloro-4-nitrophenyl beta-maltopentaosides and their application to the differential assay of human alpha-amylases
| Autor: | Shoichi Tokutake, Tetsuya Oguma, Kazunori Saito, Tobe Kouichirou, Kotani Kazuo, Nobuyuki Yamaji |
|---|---|
| Rok vydání: | 1993 |
| Předmět: |
chemistry.chemical_classification
Magnetic Resonance Spectroscopy biology Chemistry Stereochemistry Organic Chemistry Kinetics Molecular Sequence Data Glycoside Substrate (chemistry) Oligosaccharides General Medicine Biochemistry Analytical Chemistry Substrate Specificity Hydrolysis Enzyme Carbohydrate Sequence Chromogenic Compounds biology.protein Humans alpha-Amylases Alpha-amylase Saliva Pancreas |
| Zdroj: | Carbohydrate research. 238 |
| ISSN: | 0008-6215 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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