Isolation of a Plasminogen Activating Substance From Commercial Bromelain

Abstract

A procedure has been developed for the isolation of an in vitro plasminogen activating substance from the pineapple plant. A by-product of bromelain production, acetone-still residue, was used as a starting material for an isolation scheme that is initiated with reversed phase chromatography and is followed by ion exchange chromatography. The active substance appears to be a small molecule (less than 5,000 MW) with a polarity similar to aminocyclopentane carboxylic acid, based on its behavior during the above isolation scheme. It is slightly positive at pH 3.8 and is eluted along with "neutral" amino acids. The active substance has no intrinsic proteolytic activity but appears to activate one of the fibrinolytic enzymes. The plasminogen activating substance has also been isolated from commercially available bromelain. Although its mechanism of action in plasminogen activation is not known, this active substance may explain some of the physiological and clinical effects observed in bromelain.