Clinical Chemistry
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Clinical Chemistry 20: 22-25, 1974;
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Clinical Chemistry, Vol 20, 22-25, Copyright © 1974 by the American Association for Clinical Chemistry

Affinity Characteristics of Amylase-Binding Substance(s) Prepared from Macroamylase Complexes

L Fridhandler 1, J. Edward Berk 1, and Deborah Wong 1

1 Department of Medicine, California College of Medicine, University of California, Irvine, 101 City Drive South, Orange, Calif. 92668.

Partially purified macroamylase complexes, subjected to chromatography at pH 3.4, were partly or completely dissociated in each of the 30 sera so studied. The protein fractions contained variable quantities of residual undissociated macroamylase. They also contained binding substance(s), as evidenced by ability to bind added amylase. Pancreatic and salivary amylase were separately mixed with each preparation of binding substance(s) and chromatographed. Binding affinity, measured by the activity of newly formed macroamylase, varied considerably. Most of the binding substances bound considerably more salivary than pancreatic amylase; none showed markedly greater affinity toward pancreatic than toward salivary amylase. By and large, there appeared to be an association between the isoamylase pattern of the amylase released from the macroamylase complexes at pH 3.4 and the relative binding affinities of the binding substances toward pancreatic and salivary amylases.


Key Words: chromatography • pancreatic and salivary amalyses • etiology of macroamylasemia

Accepted on October 16, 1973




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A.R. Johnson
Observations on Calcium-Induced Stability of Salivary Proteins in a Lipid-Extraction System
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Copyright © 1974 by the American Association for Clinical Chemistry.