Separation of metalloprotease by ion-exchange chromatography. Proteins in CM from the AGE isolate were precipitated and fractionated using FPLC ion-exchange chromatography. A) A representative chromatogram showing a typical elution profile is shown. The collected fractions were tested for protease activity, and B) shows that fractions 10 and 11 (in the first major UV-absorbing peak) exhibited only metalloprotease activity (approx. Mw. 150 KD). Results are representative of three experiments.