Survey of α-amylase activity and isoamylases in autopsy tissue

R. O. Whitten, W. L. Chandler, M. G.E. Thomas, K. J. Clayson, J. S. Fine

Research output: Contribution to journalArticlepeer-review

17 Scopus citations


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 agerose (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 pancreas, but that their low total amylase concentrations diminish their clinical importance.

Original languageEnglish (US)
Pages (from-to)1552-1555
Number of pages4
JournalClinical Chemistry
Issue number8
StatePublished - 1988

ASJC Scopus subject areas

  • Clinical Biochemistry
  • Biochemistry, medical


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