[Studies of the manifold of amylase]

alpha-Amylase (1.4-alpha-D-glucan-glucanohydrolase, E.C 3.2.1.1) is distributed widely in animal and plant kingdoms. A number of properties of this enzyme have been recognized molecular biologically using animal organs. On the other hand, physiological roles and specificities of serum amylase are not known. The source organs of serum amylase have not been confirmed in every animal. The purposes of the experiments are to find out the specificities and varieties of amylase in some kinds of animals. The following results were obtained. 1. Amylase activities in the sera (body fluids) of some animals (Mammals, Birds, Amphibians, Fishes, Insects and Shellfish, 25 kinds altogether) were quite different from each other. The highest amylase activity except insects was observed in the serum of hamster (400 units) and the lowest was in the serum of horse (0.4 units). The activity of locust and oriental longheaded locust, eating grain mainly, was high (locust, 1965 units). 2. Five isoamylases were detected in the serum of rat. Four of them migrated to anode. 2-5 isoamylases were observed in other subjects and the mobility of isoamylases was different from each other. This seemed to be caused by the differences of isoamylase proteins. 3. Amylase activities in the brain, parotid gland, submandibular gland, sublingual gland, tongue, lung, heart, liver, stomach, spleen, pancreas, adrenal, serum and urine of hamster, rat, mouse and rabbit were measured. The activity was especially high in the parotid gland and pancreas. In rabbit, however, amylase activity in these organs was lower than that of other animals. 4. Isoamylases in some organs of four kinds of animals (hamster, rat, mouse and rabbit) were separated electrophoretically. Isoamylases in the serum of rat, hamster and mouse were similar to those in the parotid, submandibular and sublingual glands, respectively. In rabbit, it was difficult to separate isoamylases in the parotid gland and pancreas. 5. Amylases in the parotid gland and locus body were purified by column chromatography (potato starch).