Clinical Chemistry
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Clinical Chemistry 20: 673-675, 1974;
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Clinical Chemistry, Vol 20, 673-675, Copyright © 1974 by the American Association for Clinical Chemistry

Reinterpretation of Hyperamylasemia in Diabetic Coma

David M. Goldberg 1, Richard J. Spooner 1, and Anthony H. Knight 1

1 Department of Chemical Pathology and the Department of Medicine, Royal Hospital, West Street, Sheffield S1 3SR, England.

Serum enzyme activity was sequentially determined in 10 consecutive patients with diabetic ketoacidosis, of whom all had increased beta-glucuronidase activity, eight had increased amylase activity, and four had increased acid phosphatase activity. Activity of amylase and that of the two lysosomal enzymes were poorly correlated, irrespective of whether peak activities or activities of all samples were considered. Of 37 cases with acute viral hepatitis, serum beta-glucuronidase activity was increased in 33 and amylase activity in four, and the correlation between the two was poor. Study of normal human liver showed that the ratio of its mean enzymatic activity to the upper normal limit for serum was less than 1.0 for amylase, and approximately 80 and 6000 for acid phosphatase and beta-glucuronidase, respectively. The hepatocyte cannot be the source of an increased serum amylase activity, and we question whether lysosomes are concerned in its release from other tissues.


Key Words: lysosomal enzymes • origin of serum amylase activity • diabetic ketoacidosis • viral hepatitis

Submitted on February 11, 1974
Accepted on April 2, 1974




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 ANN INTERN MEDHome page
F. VINICOR, L. M. LEHRNER, R. C. KARN, and A. D. MERRITT
Hyperamylasemia in Diabetic Ketoacidosis: Sources and Significance
Ann Intern Med, August 1, 1979; 91(2): 200 - 204.
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Copyright © 1974 by the American Association for Clinical Chemistry.