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J. Biochem, 1974, Vol. 76, No. 6 1235-1242
© 1974 Japanese Biochemical Society

research-article

A Glucose-forming Amylase in Human Liver

Kazuaki TSUJINO, Masao YOSHIMURA*, Kimio UMEKI**, Noshi MINAMIURA** and Takehiko VAMAMOTO**

Osaka City University, School of Medicine
*Osaka Medical Examiners' Office
**Osaka City University, Faculty of Science

An amylase preparation free from {alpha}-amylase [EC 3.2.1.1 [EC] ] activity was obtained from human liver and its properties were investigated. The amylase hydrolyzed maltose and malto-oligosaccharides, liberating glucose from the non-reducing terminal. The enzyme also hydrolyzed starch, glycogen, and ß-limit dextrin to a considerable extent, producing only glucose, though it was unable to hydrolyze isomaltose. However, the enzyme specificity was distinguished from that of glucoamylase [EC 3.2.1.3 [EC] ] of microbial origin in that the former had a much higher activity toward maltose than toward glycogen and starch. On the other hand, the liver glucose-forming amylase was similar to an isozyme of urine glucose-forming amylases in several enzymic and physicochemical properties.


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