Influence de l'α2-macroglobuline du lapin sur l'activite enzymatique de la trypsine et de la chymotrypsine

Abstract

1.1. The rabbit α2 macroglobulin (α2 M) can bind trypsin and chymotrypsin with the formation of an enzymatically active complex. The links are strong enough to resist gel filtration.2.2. The effect of α2 M on the esterolytic activities of trypsin and chymotrypsin was investigated using benzoyl-arginine ethyl-ester, p-tosyl-l-arginine methyl ester and acetyl-tyrosine ethyl ester as substrates.3.3. Michaelis constants of the complexes were determined by the method of Eadie (1942). The proteolytic activity was investigated using caseine as a substrate.4.4. The competition of trypsin and chymotrypsin for the association site was studied and the ability of the α2 M to protect these enzymes from soybean trypsin inhibitor was determined.5.5. One mole of α2 M binds 2 moles of trypsin or chymotrypsin.6.6. Rabbit α2 M has numerous similarities with rabbit α1 M.