Clinical Chemistry, Vol 34, 1552-1555, Copyright © 1988 by American Association for Clinical Chemistry

Survey of alpha-amylase activity and isoamylases in autopsy tissue

RO Whitten, WL Chandler, MG Thomas, KJ Clayson and JS Fine
Department of Laboratory Medicine, University of Washington, Seattle 98195.

We quantified total amylase and its isoenzymes in 22 different human tissues obtained at autopsy. Isoenzymes were separated by use of wheat- germ inhibition (WI) and electrophoresis on cellulose acetate (CA) and agarose (AG). Mean (+/- SD) total activity was highest in salivary glands (parotid 1710 +/- 897 U/g, submandibular 605 +/- 354 U/g), and pancreas (258 +/- 137 U/g). All other tissues contained 100- to 1000- fold less amylase. As assessed with WI, pancreas, jejunum, liver, placenta, testis, skeletal muscle, and spleen contained more than 90% pancreatic isoamylase. Salivary glands and thyroid contained more than 90% salivary isoamylase. All other tissues contained a mixture of the two isoenzymes. CA and AG often produced different results. For both CA and AG the most common pancreatic isoforms were P2 and S1. Salivary gland homogenates demonstrated a band migrating in the P3 position on CA. We conclude that both types of amylase isoenzymes can be found in tissues other than salivary gland and pancreas, but that their low total amylase concentrations diminish their clinical importance.

The following articles in journals at HighWire Press have cited this article:

				S. M. Kurzweil, M. J. Shapiro, C. H. Andrus, C. M. Wittgen, V. M. Herrmann, and D. L. Kaminski Hyperbilirubinemia Without Common Bile Duct Abnormalities and Hyperamylasemia Without Pancreatitis in Patients With Gallbladder Disease Arch Surg, August 1, 1994; 129(8): 829 - 833. [Abstract] [PDF]

				M. H. Meisler and C.-N. Ting The Remarkable Evolutionary History of the Human Amylase Genes Critical Reviews in Oral Biology & Medicine, January 1, 1993; 4(3): 503 - 509. [Abstract] [Full Text] [PDF]