Separation of Arginine Amidases Released from the Isolated Rabbit Aorta

Abstract

The extract from isolated rabbit aortae were added to a Krebs solution for 1 h to secrete enzymes. Then, the arginine amidase activity identified in the obtained sample solution was separated using affinity adsorption on lysine-, anti-thrombin lll- and aprotinin conjugated columns. Enzymes adsorbed on lysine and aprotinin affinity columns were found in the extract of isolated rabbit aortae. On the other hand, few enzymes showing affinity with the anti-thrombin lll column were detected. Two forms of arginine amidases with different affinities were isolated and these showed different substrate specificities. The arginine amidase obtained from the lysine affinity column was supposed to be plasmin because it was completely inhibited by antiplasminogen.