PURIFICATION OF SECRETED PLATELET PROTEASE NEXIN-I

Authors
Citation
K. Chen et Dw. Essex, PURIFICATION OF SECRETED PLATELET PROTEASE NEXIN-I, Thrombosis research, 79(5-6), 1995, pp. 527-529
Citations number
8
Categorie Soggetti
Hematology,"Cardiac & Cardiovascular System","Peripheal Vascular Diseas
Journal title
ISSN journal
00493848
Volume
79
Issue
5-6
Year of publication
1995
Pages
527 - 529
Database
ISI
SICI code
0049-3848(1995)79:5-6<527:POSPPN>2.0.ZU;2-2
Abstract
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.