Abstract
Pancreatic and urinary kallikreins failed to form the typical serine proteinase complex with [human] .alpha.2M (.alpha.2-macroglobulin). Studies were performed to compare this with the binding of trypsin to .alpha.2M at various molar binding ratios, with the use of Sephadex G-200 gel filtration to separate free and .alpha.2M-bound enzyme fractions. The subunit conversion was totally absent with pancreatic kallikrein from which traces of a binding proteinase had been removed. The lack of binding is probably the result of the restricted specificity of the kallikreins.