Abstract
Rabbit liver proteolysis was studied, yielding the following results:
1. Enzyme solution which is incubated at pH 8.2-8.6 at 37°C for thirty or forty minutes exhibits tryptase activity (casein, gelatin, pH 7.8) and ereptase activity (pepton, pH 7.8) but does not exhibit catheptic proteinase and catheptic peptonase activity (casein, gelatin or pepton, pH 4.5, with cystein activation).
2. Tryptase is rather inhibited by cystein but ereptase is not.
3. Enzyme solution which is incubated at pH 3.5 at 37°C for forty minutes exhibits only tryptase activity, and neither ereptase nor catheptase activity can be observed on it.
4. Tryptase activity appears to increase slightly after incubation at pH 4.0-4.5 at 37°C.
5. Enzyme solution which is incubated at pH 9.0 at 37°C for sixty minutes exhibits ereptase activity, and neither catheptase nor tryptase activity can be observed on it.
6. Existence on rabbit liver of tryptase is definitely evidenced.
This work was carried out by a Grant for Development of Scientific Researches given from the Ministry of Education. M. Hayakawa
