抄録
One form of calcium-activated neutral protease (CANP) highly sensitive to calcium ions was purified by column chromatographic procedures to homogeneity. The purified enzyme required μM order Ca2+ (μCANP), and the half-maximum activity was attained at 50 μM Ca2+. The electrophoretic mobility in a non-denaturing buffer showed that this enzyme is less acidic than another CANP which required mM order Ca2+ (mCANP). On SDS-polyacrylamide gel electrophoresis, the enzyme separated into two components with molecular weights of 79, 000 and 28, 000, respectively. Of these, the former was slightly larger than the counterpart of mCANP (Mr 76, 000). Thus, pCANP cannot be derived from mCANP by limited autolysis.
