By O. Lowenstein
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Extra resources for Advances in Comparative Physiology and Biochemistry
The evidence for and against human liver amylase has been addressed in a recent review of human α-amylases (Merritt and Karn, 1977). In summary, claims have been made for the existence of human amylase, immunologically distinct from that produced in the pancreas and salivary glands, which is synthesized in the liver and contributed to the serum and urine (McGeachin and Reynolds, 1961). In attempting to repeat and extend that observation, Karn et al. (1976) showed that the immunologically distinct amylase was actually a spu rious activity produced in the amyloclastic assay by the presence of al bumin in serum and tissue extracts.
1971) compared mammalian amylases by disc electrophoresis followed by indirect staining on starch plates (Fig. 14). In comparing saliva, serum, urine, pancreatic extracts, and extracts of the small intestine, they found multiple electrophoretic forms in nearly all sources. Specific studies employing a variety of electrophoretic techniques have revealed fur ther heterogeneity in many of these organisms. , 1975), and the house fly (Ogita, 1968) have been the subjects of electrophoretic studies of amylase.
The vertebrate pan creas secretes numerous hydrolytic enzymes, among them a-amylase. This is probably the most indisputable source of the enzyme in this group of animals (Table VI). Salivary α-amylase secretion, however, is relatively restricted in vertebrates, having been reported only in frogs, rodents, primates, and the prototherian mammal echidna (Griffiths, 1965). In the echidna and the grasshopper mouse, saliva is the primary source of amylase secretion, and its action occurs mainly in the stom ach which has a neutral, rather t h a n acid, pH (Barnard and Prosser, 1973).
Advances in Comparative Physiology and Biochemistry by O. Lowenstein