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The unique mo­ bility was attributed to the mobility of glycogen which is much larger than the enzyme. Glycogen does have some electrophoretic mobility apparently due to electroendosmotic flow. Finally, Takeuchi and his colleagues (1975b) showed that the amylase isozyme from the livers of either well-fed or fasted rats cross-reacted immunologically with sali­ vary amylase but not with pancreatic amylase. They concluded that liver amylase was the result of contamination of liver extracts with salivary-type amylase which occurs in the serum.

For example, a comparison of primate parotid amy­ lases and Drosophila amylases reveals significant differences in many of the amino acid residues. A definitive analysis of the terminal residues of hog pancreatic amylase has been reported by Romano and Strumeyer (1976) who em­ ployed a protease-free preparation of pancreatic amylase for their studies. No free amino terminal residues were observed when several methods were used, including reaction with fluorodinitrobenzene, trinitrobenzenesulfonic acid, dansyl chloride, and cyanate.

By combining their chemical studies with genetic studies (see Section VI), they were able to distin­ guish the primary allelic products of different phenotypes from the products of posttranslational modifications. One of the most thoroughly studied animal amylases is the pancre­ atic amylase of the hog. Unfortunately, little is known about hog serum and other potential amylase-containing tissues and fluids. The only comparative electrophoretic studies available are those of Rajasingham et al. (1971) showing electrophoretic patterns of salivary gland, serum, urine, pancreas, small intestine, and liver isozymes (Fig.

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