Abstract
Summary
Observations on the behavior and nature of the macroamylase found in 12 patients with macroamylasemia lend further support to the earlier suggestion that the macromolecular amylase component is not homogenous. This was evidenced by variation in the relative amounts of macroamylase present in the serum and differences in the elution patterns obtained following dextran gel filtration. Disappearance or marked diminution of the macroamylase after exposure to urea would suggest that the macroamylase consists either of a polymer of normal serum amylase or a combination of normal serum amylase and a larger protein molecule. The active portion of the macroamylase complex appears to differ only slightly, if at all, from normal serum amylase regardless of the protein fraction with which it may be associated. Immunoglobulins may be involved with the complex in some but seemingly not in all cases.
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