| Abstract: | Donkey antiserum to normal human pancreas absorbed with lyophilized human plasma recognized human urokallikrein in concentrated crude urine or after an approximately 500-fold purification. The urokallikrein antigen was associated with kinin-generating and alpha-N-p-tosyl-L-arginine methyl ester (TAMe) cleaving activity on isoelectric focusing, with the isoelectric point being 3.8 to 4.4. Both kiningenerating and esterolytic activity were removed from the purified urokallikrein by an immunoadsorbent prepared by coupling the IgG fraction of the absorbed donkey antiserum to Sepharose 6B. The failure of anti-plasma kallikrein to react in immunodiffusion with purified urokallikrein indicates that urinary kallikrein is distinct from plasma kallikrein although antigenically related to glandular kallikreins. |
