Maltotetraose-forming, amylase-mediated, p-nitrophenyl α-and β-maltopentaoside formation in an aqueous—organic solvent system: a substrate for human amylase in serum-Reference-Cited by-同舟云学术

Maltotetraose-forming, amylase-mediated, p-nitrophenyl α-and β-maltopentaoside formation in an aqueous—organic solvent system: a substrate for human amylase in serum

Published:1991-06 Issue: Volume:212 Page:289-294
ISSN:0008-6215
Container-title:Carbohydrate Research
language:en
Short-container-title:Carbohydrate Research

Author:

Ogawa Koichi,Murata Takeomi,Usui Taichi

Publisher

Elsevier BV

Subject

Organic Chemistry,Biochemistry,General Medicine,Analytical Chemistry

Reference14 articles.

1. Direct spectrophotometric determination of alpha-amylase activity in salive, with p-nitrophenyl alpha-maltoside as substrate.

2. Mechanism of action of human pancreatic and salivary alpha-amylase on alpha-4-nitrophenyl maltoheptaoside substrate.

3. Differential Rate Assay of Human Pancreatic and Salivary α-Amylases in Serum Using Two Coupled Enzymes

4. Synthesis of p-nitrophenyl 65-O-benzyl-α-maltopentaoside, a substrate for alpha amylases

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