TRYPSINIZATION OF DERIVATIVES OF CLOSTRIDIUM-PERFRINGENS ENTEROTOXIN

Three proteins, named P1, P2 and P3, were separated from purified Clostridium perfringens enterotoxin by high performance liquid chromatography (HPLC) on a DEAE-SPW column. The relative biological activities of P1, P2 and P3 on protein basis determined by the African green monkey kidney (Vero) cell staining assay were 3.0, 1.9 and 1.0, respectively. P1, when trypsinized and re-chromatographed, revealed the same HPLC pattern as that of untrypsinized P1, but a new peak, P2, emerged from P2 and P3 after trypsinization, by HPLC. The relative biological activity of trypsinized P1 was of the same level as that of untreated Pi, but those of P2 and P3 increased one and a half to three times upon trypsinization and finally reached the same level as those of P1 and P2'. © 1986 Oxford University Press. All rights reserved.