Thrombin, a platelet agonist which also has biological effects towards
other cells, forms complexes with platelet proteins which may affect
its activity (1). One such complex with platelet protease nexin is for
med in the supernatant solution of activitated platelets and has an ap
parent mass of 77 kd (2,3,4). Protein nexin I also forms a similar siz
e complex with thrombin (5). However, apparent differences between the
se two nexins (4), as well as difficulties in purifying the platelet n
exin, have prevented the identification of the platelet nexin. We puri
fied the nexin from the supernatant solution of activated platelets an
d identified it as protease nexin I (PNIp). The two components in the
77 kd complex are thrombin and PNIp.