Carbohydrate research

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

K Ogawa, T Murata, T Usui

Index: Ogawa, Koichi; Murata, Takeomi; Usui, Taichi Carbohydrate Research, 1991 , vol. 212, p. 289 - 294

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Citation Number: 21

Abstract

In recent years, malto-oligosaccharide derivatives of defined structure have been used in clinical laboratories'” for the measu rement of alpha-amylase activity in human serum and urine. One such chromogenic substrate2.'is pNP-aG,. However, conventional methods for obtaining pNP-aG,, either chemically or enzymically, give only low yields of the desired compound 8q9 We have reported that G,-amylase from Pseudomo-. nas stutzeri forms ...