A novel protein accumulated during maturation of the pods of the plant Impatiens balsamina.

A high molecular weight protein has been isolated as a major polypeptide comprising 85% of the total extractable proteins in the fruit pericarp of the plant Impatiens balsamina. The protein has been purified to homogeneity following fractionation of the crude cell supernatant with ammonium sulphate, chromatography on Sepharose 4B and Sephacryl-S-300. This protein appeared to be a homo-tetramer consisting of subunits, Mr 75 K. Amino acid analysis showed the presence of more acidic amino acids, with an isoelectric point 5.8. The interaction of this protein with filamentous actin, both from rabbit muscle and Mung bean embryo was monitored by transmission electron microscopy, light scattering analysis, viscometry and sedimentation assay. This protein inhibited appreciably the polymerization of G-actin to F-actin.