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Clinical Chemistry 30: 1219-1222, 1984;
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Clinical Chemistry, Vol 30, 1219-1222, Copyright © 1984 by American Association for Clinical Chemistry

Automated measurement of amylase isoenzymes with 4-nitrophenyl- maltoheptaoside as substrate and use of a selective amylase inhibitor

H Okabe, Y Uji, K Netsu and A Noma

We automated a kinetic procedure for determining amylase isoenzymes in serum and urine samples. We used 4-nitro-phenylmaltoheptaoside as substrate and a selective amylase inhibitor with the Abbott-VP bichromatic system. By use of the maximum differences between pancreatic (P) and salivary (S) amylase activities remaining after inhibition by the selective inhibitor and by use of the linear range, a one-point standard method for calibration is proposed for determining amylase activities between about 50 and 1500 U/L when the P/S ratio exceeds 0.2. Results correlated well with those by electrophoresis and the Phadebas method (r = 0.99 for both pancreatic and salivary amylase). Reproducibilities (CVs) were 1.5% to 5.5% for pancreatic amylase and 1.4% to 3.3% for salivary amylase in serum, 0.8% to 2.0% for pancreatic amylase and 0.8% to 2.3% for salivary amylase in urine.


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ANN INTERN MEDHome page
L. L. HUMPHRIES, L. J. ADAMS, J. H. ECKFELDT, M. D. LEVITT, and C. J. McCLAIN
Hyperamylasemia in Patients with Eating Disorders
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ANN INTERN MEDHome page
J. H. ECKFELDT, J. W. LEATHERMAN, and M. D. LEVITT
High Prevalence of Hyperamylasemia in Patients with Acidemia
Ann Intern Med, March 1, 1986; 104(3): 362 - 363.
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Arch Intern MedHome page
J. H. Eckfeldt and M. J. Kershaw
Hyperamylasemia Following Methyl Alcohol Intoxication: Source and Significance
Arch Intern Med, January 1, 1986; 146(1): 193 - 194.
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Copyright © 1984 by the American Association for Clinical Chemistry.