Neutrophil procollagenase (MMP-8) was efficiently activated by incubation with active stromelysin 2 (MMP-10). A single-step activation mechanism involving the cleavage of the Gly78-Phe79 peptide bond at the end of the propeptide domain was observed. Determination of the collagenolytic activity revealed the generation of active neutrophil collagenase displaying high specific activity. When compared with the specific activity following mercurial activation, which generates active collagenase by autoproteolytic cleavage of either Phe79-Met8O or Met8O-Leu81 peptide bonds [Bläser, J., Knäuper, V., Osthues, A., Reinke, H. & Tschesche, H. (1991) Eur J. Biochem. 202, 1223-1230], the specific activity of the stromelysin-2-activated enzyme was considerably higher. Thus, human neutrophil procollagenase was 'superactivated' by stromelysin 2, as was recently shown for the stromelysin-1-activated enzyme [Knäuper, V., Wilhelm, S. M., Seperack, P. K., De Clerck, Y. A., Langley, K. E., Osthues, A. & Tschesche, H. 1993 a) Biochem. J. 295, 581-586].