Department of Biochemistry, University of Washington, Seattle, WA 98195 USA
Abstract:
Affinity chromatographic systems are described for the purification of neutral metalloendopeptidases on columns of acetyl--phenylalanine or succinyl--leucine covalently linked to Sepharose by spacers of various lengths. The neutral proteases of are separated in a single chromatographic procedure from all other proteins of the culture filtrates and subfractionated into two active species. An analogous chromatographic system is effective in the purification of thermolysin of .