alpha-Amylase of human pure pancreatic juice: effects of pancreatic disease and the occurrence of variant forms in pancreatic juice from healthy volunteers.

Pure pancreatic juice (PPJ) from healthy human volunteers and from patients with pancreatic or liver disease was subjected to isoelectric focussing (IEF) and assayed for alpha-amylase activity. In PPJ from most normals, a single predominant form of amylase was found, comprising congruent to 83% of the total activity recovered, and having pIapp congruent to pH 6.8. In PPJ from six normals, variant principal forms of amylase were found at pH congruent to 6.4 or pH congruent to 7.3, in addition to the peak at pH 6.8. IEF patterns of PPJ from individuals with pancreatic or liver disease were indisquishable from patterns obtained with PPJ from the control group of healthy volunteers.