NDLI: Action Pattern of Human Pancreatic and Salivary α-Amylase on 1,4-α-D-Nitrophenylmaltooligosaccharides. 1,4-α-D-Nitrophenylmaltooligosaccharides as Substrates of α-Amylase, I

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Action Pattern of Human Pancreatic and Salivary α-Amylase on 1,4-α-D-Nitrophenylmaltooligosaccharides. 1,4-α-D-Nitrophenylmaltooligosaccharides as Substrates of α-Amylase, I

Content Provider	Scilit
Author	Wallenfels, K. Laule, G. Meltzer, Barbara
Copyright Year	1982
Abstract	High performance liquid chromatography (HPLC) was used to monitor the purity of the substrates and to establish the patterns of hydrolysis of ortho- and para-nitrophenylmaltooligosaccharides (2-7 glucose residues) catalysed by human pancreatic and salivary alpha-amylase. Separation of the reaction products from the remaining substrate was performed on a TSK-G-2000 PW or a RP18 column. By measuring the quantitative distribution of products, and assuming a 5-subsite model for the active site of alpha-amylase, differential activities for the hydrolysis of the different glycosidic bonds in the 2 series of substrates were deduced. A highly sensitive coupled continuous assay system is based on the formation of phenyloligosaccharides with 1-4 glucose residues by the action of the amylase under test, coupled to hydrolysis of these products by yeast alpha-glucosidase. The most suitable test substrates were shown to be para-nitrophenyl-alpha-D-maltotetraoside and -pentaoside. Direct production of nitrophenol from ortho-nitrophenyl-alpha-D-maltotrioside is recommended for the measurement of the alpha-amylase activity of pancreatic and salivary gland secretions and extracts.
Related Links	http://www.degruyter.com/downloadpdf/j/cclm.1982.20.issue-8/cclm.1982.20.8.581/cclm.1982.20.8.581.xml
Ending Page	586
Page Count	6
Starting Page	581
ISSN	14346621
e-ISSN	14374331
DOI	10.1515/cclm.1982.20.8.581
Journal	Clinical Chemistry and Laboratory Medicine (CCLM)
Issue Number	8
Volume Number	20
Language	English
Publisher	Walter de Gruyter GmbH
Publisher Date	1982-01-01
Access Restriction	Open
Subject Keyword	Clinical Chemistry and Laboratory Medicine (cclm) Biochemical Research Analytical Chemistry Model Differential Substrates Ortho Alpha Amylase Nitrophenylmaltooligosaccharides Journal: Clinical Chemistry and Laboratory Medicine (CCLM), Vol- 20
Content Type	Text
Resource Type	Article
Subject	Biochemistry (medical) Clinical Biochemistry

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