[Study of the complex between porcine plasmin and alpha2-macroglobulin (author's transl)].

Porcine plasmin (EC 3.4.21.

[Not Available].

Tryptic hydrolysis of different arginine nitroanilides was studied. Para-nitroanilide is the most readily hydrolyzed substrate, ortho derivative is 5 times less sensitive and meta derivative is a very weak substrate. When the benzoyl group bound on the N(alpha) arginine of BAPNA is replaced by a carbobenzoxy group (L-ZAPNA), the tryptic hydrolysis is increased by a factor of 3.

[Not Available].

The complex formed between trypsin and alpha(2)-macroglobulin retains the whole hydrolytic activity for benzoylarginine-p-nitroanilide (DL BAPNA). We have observed that the inhibition of this activity is dependent on the inhibitor used. While soya bean inhibitor (MW = 20 000) is ineffective, the basic pancreatic inhibitor (MW = 6 500) progressively inhibits the complex.