Zur Auftrennung und Charakterisierung proteolytischer Enzyme aus Euglena gracilis

Summary To test the activities of proteolytic enzymes in Euglena gracilis Klebs (1224 — 5/25, strain Z) some procedures of cell destruction were compared. Destruction with Alcoa A 305 had been most suitable. In separation of the proteolytic enzyme spectrum Sephadex G-200 showed the best results. The following activities were differentiated: 1. Amino acid arylamidase I (splits Leu-NA better than Ala-NA, except on the p H-optimum (for Leu 7,3, for Ala 7,7) and better than Arg-NA ( p H-optimum 7,1). 2. L-Leucine aminopeptidase (splits Leu-NH 2 and Leu-Gly-Gly; activated by Mn 2+ ). 3. Amino acid arylamidase II (less activity than I, splits Ala-NA always better than Leu-NA better than Arg-NA). 4. L-aminoacid acylase (splits acetyl- and chloracetyl-aminoacids on p H 8,2—8,4; the enzyme is independent of metal ions; molecular weight about 78.000). 5. L-amino tri(poly)peptidase (splits on p H 7.8 Leu-Gly-Gly and similar tripeptides as well as Gly-Gly-D-Leu; inhibition by Mn 2+ ). 6. Acid carboxypeptidase (splits Z-L-dipeptides or tripeptides on p H 4,5 —5,7). 7. L-aminoacyl-L-aminoacid-hydrolase (dipeptidase).