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On human serum amylase

Authors:	E Afonso

Affiliation:	1. Reconstructive Surgery and Regenerative Medicine Group, Swansea University, Swansea, United Kingdom;2. Centre for Nanohealth, Swansea University, Swansea, United Kingdom;4. Swansea University Medical School, Swansea University, Swansea, United Kingdom;3. The Welsh Centre for Burns and Plastic Surgery, Morriston Hospital, Swansea, United Kingdom;1. Centre for Nanotechnology, Indian Institute of Technology Guwahati, Assam 781039, India;2. Department of Chemistry, Indian Institute of Technology Guwahati, Assam 781039, India;3. Department of Chemical Engineering, Indian Institute of Technology Guwahati, Assam 781039, India;4. Department of Chemical Engineering, Indian Institute of Technology Guwahati, 781039, Assam, India

Abstract:	Human serum amylase was studied by agar gel electrophoresis and quantitative immunoelectrophoresis. Two fractions having slightly different β₂-γ mobilities were found in normal sera. No isoenzyme type of association or binding with normally precipitating immunoelectrophoretic fractions were found. The two fractions are designated as A₁ (slower) and A₂ (faster) according to their relative mobilities towards the anode. A₁: fraction was found to be greatly increased in a case of acute pancreatitis which showed a characteristic pattern in quantitative immunoelectrophoresis.

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