Abstract:
:Plasma hyaluronan biding protein (PHBP) is a novel serine protease, which has an amino acid sequence homology to that of hepatocyte growth factor activator (HGFA), and has a similar domain structure to that of urinary plasminogen activator (u-PA), found in human plasma. We searched the PHBP substrate in human plasma by measuring the digested protein bands on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The results showed that fibrinogen and fibronectin were the major substrates of PHBP. PHBP cleaved the alpha-chain at multiple sites and the beta-chain between lysine53 and lysine54 but not the gamma-chain of fibrinogen. Therefore, PHBP did not initiate the formation of the fibrin clot and did not cause the fibrinolysis directly. PHBP did not cleave (activate) prothrombin and plasminogen, but it converted the inactive single chain urinary plasminogen activator to the active two chain form.
journal_name
Biol Pharm Bulljournal_title
Biological & pharmaceutical bulletinauthors
Choi-Miura NH,Yoda M,Saito K,Takahashi K,Tomita Mdoi
10.1248/bpb.24.140subject
Has Abstractpub_date
2001-02-01 00:00:00pages
140-3issue
2eissn
0918-6158issn
1347-5215journal_volume
24pub_type
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