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1 Department of Oral Pathology, School of Pathology, University of the Witwatersrand and South African Institute for Medical Research, Johannesburg, South Africa
A starch substrate film technique was used for the qualitative histochemical demonstration of amylase in normal and diseased human salivary glands and in the normal glands of the rat, mouse, and dog. Amylase activity was demonstrable apical to the nuclei in the acinar cells of the human, rat, and mouse parotid glands and in the serous cells of the human submaxillary gland. In the rat submaxillary gland, amylase was observed only in the large vessels and fine capillaries in both fasting animals and after pilocarpine administration. Atrophic serous acini in human submaxillary glands, which have been exposed to ionizing radiation, appeared to have the ability to synthesize amylase. This enzyme also was present in developing acini in human neonate parotid glands. This amylase technique was quantitated on rat parotid glands by assaying activity in serial sections. Activity was expressed as milligrams maltose per micrograms protein in a section after five minute incubation at 37 C. A gelatin substrate film technique was used for the qualitative histochemical demonstration of protease. This enzyme was present in the granular convoluted tubules of rat and mouse submaxillary glands, and in fat cells in all salivary glands.
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