Abstract
To increase specificity in the clinical determination of amylase, the differential activities of human pancreatic and salivary amylases toward two different substrates—a Lintner soluble starch (LSS) and an insoluble, dyed starch, Amylose Azure (AA)—were investigated. A ratio of initial-velocity activities of Lintner soluble starch to Amylose Azure (LSS/AA) for salivary amylase was at least twice as great as the LSS/AA ratio obtained for pancreatic amylase. Statistical analysis of paired saliva samples and secretin-pancreozymin stimulated pancreatic juices revealed a significant (p < 0.01) difference between the mean LSS/AA activity ratios of these two biologic fluids. Even greater differences were found between the ratios for crystalline salivary amylase compared to the amylase contained in purified preparations from human duodenal fluid and pancreatic homogenates. A method to differentiate elevated serum amylase resulting from parotitis or pancreatitis is demonstrated.
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Supported in part by Grant AM 12722 of the NIH, US Public Health Service.
The authors thank Mrs. Edith Austin and Mr. Joe Jeter for technical assistance and Mrs. Monica Drobena for typing this manuscript. Special thanks are extended to Dr. M. S. Urista, Chief, Laboratory Service, VA Hospital, Temple, Texas, for procuring the human pancreases, and to Dr. T. D. Tanksley, Professor, Animal Science Department, Texas A & M University, College Station, Texas, for obtaining the hog saliva.
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Hall, F.F., Ratliff, C.R., Hayakawa, T. et al. Substrate differentiation of human pancreatic and salivary alpha-amylases. Digest Dis Sci 15, 1031–1038 (1970). https://doi.org/10.1007/BF02232822
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DOI: https://doi.org/10.1007/BF02232822