Purification and Properties of a Protein Activator of Human Pancreatic Lipase

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Abstract
A protein activator for human pancreatic lipase [EC 3.1.1.3] was purified from human pancreatic juice. The purified activator appeared to be homogeneous by ultracentrifugal and disc gel electrophoretic criteria. The molecular weight of the activator was determined by sodium dodecylsulfate-polyacrylamide gel electrophoresis to be about 13,000. The purified activator lost its activity on digestion with trypsin [EC 3.4.21.4]. The purified activator was found to be a glycoprotein. Addition of the activator stimulated 6- to 10-fold the activity of purified human pancreatic lipase which had been inactivated by dilution of the enzyme with 0.05 M Tris-HC1 buffer (pH 8.6) at 25°. This activation by the protein activator was found to depend on the presence of Ca2+ and sodium deoxycholate. The present results suggest that Ca2+ may bind to the protein activator and then this complex activates the inactivated enzyme.

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