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A cell wall lytic enzyme of Chlamydomonas reinhardtii has been purified and identified as a single glycopolypeptide subunit of 62 kDa by SDS-polyacrylamide gel electrophoresis. It is released into culture medium by mating gametes as a large aggregate of subunits. The purified enzyme shows a pH optimum at about 7.5 and 35 o C. Metal ion chelators and SH-blocking agents inhibit the activity. The activity is also diminished by α 2 -macroglobulin.