• Saroj Sapkota
  • Ebenezer William


Objective: Enzyme amylase in humans is a digestive enzyme that acts to cleave starch into smaller carbohydrates. The iso-enzymes of amylase are
salivary (S) type and pancreatic (P) type with different characteristics properties. Hyperamylasemia is a condition with increased total serum amylase
activity. It is often difficult to interpret the actual defective source with a total serum amylase activity. Therefore, this study of iso-amylase patterns by
electrophoretic technique aids in recognizing the correct source of origin of the enzyme amylase.
Methods: A total of 80 subjects aged ranges from 20-60 years were recruited from SRM Medical College Hospital and Research center, Tamil
Nadu. The subjects included were subdivided as Group 1 of 20 acute pancreatitis, Group 2 of 20 diabetes mellitus, Group 3 of 20 cholecystitis and
Group 4 of 20 normal healthy subjects. Serum samples were obtained and analyzed in autoanalyzer and subjected to agarose gel electrophoresis for
electrophoretic separation of isoamylase bands.
Results: Total serum amylase activity was measured. Electrophoretic iso-enzyme patterns of serum amylase of normal healthy person showed a narrow
band of S-type toward the anode, followed by the P-type from the point of application. Electrophoresis of sera of pancreatitis showed only a single
prominent P-type band, cholecystitis sera showed a thin S-type with P-type band and diabetic sera had a broad S-type and thin P-type isoamylase bands.
Conclusion: Agarose gel electrophoresis is a simple technique and can be run with minimal efforts. The isoamylase band patterns observed differentiates
the source of origin of serum amylase. Thereby aids the physicians to take the next right leading step and decide necessary further investigations.

Keywords: Isoamylase, Hyperamylasemia, Agarose gel electrophoresis.


1. Frossard JL, Steer ML, Pastor CM. Acute pancreatitis. Lancet
2. Panteghini M, Bais R. Enzymes. Burtis CA, Ashwood ER, Bruns DE,
editors. Tietz Textbook of Clinical Chemistry and Molecular
Diagnostics. 4th ed. St. Louis, MO: Saunders; 2008.
3. Skrha J, Stephan J. Clinical significance of amylase isoenzymes
determination. Acta Univ Carol Med Monogr 1987;176:1-18.
4. Hsiu J, Fischer EH, Stein EA. Alpha-amylases as
calcium metalloenzymes. ii. calcium and the catalytic activity.
Biochemistry 1964;3:61-6.
5. Karn RC, Rosenblum BB, Ward JC, Merritt AD, Shulkin JD.
Immunological relationships and post-translational modification
of human salivary amylase (Amy) and pancreatic amylase (Amy)
isozymes. Biochem Genet 1974;12(6):485-99.
6. Leach BS, Collawn JF Jr, Fish WW. Behavior of glycopolypeptides
with empirical molecular weight estimation methods 1. In sodium
dodecyl sulfate. Biochemistry 1980;19(25):5734-41.
7. Royse VL, Jensen DM. Agarose gel electrophoresis technique for
determination of amylase isoenzymes. United State Patent; 1985.
8. Gillard BK, Simbala JA, Goodglick L. Reference intervals for amylase
isoenzymes in serum and plasma of infants and children. Clin Chem
9. Lebenthal E. Role of salivary amylase in gastric and intestinal digestion
of starch. Dig Dis Sci 1987;32(10):1155-7.
10. Bossuyt PJ, Van den Bogaert R, Scharpé SL, Van Maercke Y. Relation
of age to isoenzyme pattern and total activity of amylase in serum. Clin
Chem 1981;27:451-4.
11. Sneha JA, Chaudhari S. Alpha-amylase inhibitory and hypoglycemic
activity of Clerodendrone multiflorum linn stems. Asian J Pharm Clin
Res 2011;4(2):99-102.
12. Narkhede MB. Evaluation of alpha-amylase inhibitory potential of four
traditional culinary leaves. Asian J Pharm Clin Res 2012;5(2):75-6.
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How to Cite
KA, A. S., S. Sapkota, and E. William. “ISO-AMYLASE ELECTROPHORETIC PATTERNS IN HYPERAMYLASEMIC CONDITIONS ô€ˆƒ A LEADING FOOTPRINT”. Asian Journal of Pharmaceutical and Clinical Research, Vol. 8, no. 1, Jan. 2015, pp. 83-85,
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