1973
DOI: 10.1182/blood.v41.1.105.105
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Effects of Plasmin on Human Factor VIII (AHF)

Abstract: Highly purified, fibrinogen-free human factor VIII was incubated with plasmin, and the liberated split products of the factor VIII were analyzed by gel filtration, acrylamide gel electrophoresis, bioassay, and for immunologic reactivity. At least three fragments retaining different antigenic determinants are released from the factor VIII after prolonged digestion and at least three new fragments are seen in acrylamide gel electrophoresis. The split products were not anticoagulant in the factor VIII activity as… Show more

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Cited by 45 publications
(5 citation statements)
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“…Plasmin is a two‐chain macromolecule joined by two disulphide bridges (94,95) with a broad specificity protease (96–99), that cooperates with fibrin to form a clot. The role of plasmin in tumour cell invasion and migration is well documented (100–102), with evidences for both direct (by degrading proteins of the extracellular matrix and activating plasminogen activators) and indirect action (by activating of matrix metalloproteases).…”
Section: Inhibition Of Serine Proteases Activity By Polyphenolsmentioning
confidence: 99%
“…Plasmin is a two‐chain macromolecule joined by two disulphide bridges (94,95) with a broad specificity protease (96–99), that cooperates with fibrin to form a clot. The role of plasmin in tumour cell invasion and migration is well documented (100–102), with evidences for both direct (by degrading proteins of the extracellular matrix and activating plasminogen activators) and indirect action (by activating of matrix metalloproteases).…”
Section: Inhibition Of Serine Proteases Activity By Polyphenolsmentioning
confidence: 99%
“…Associated with VIII:C in plasma is a protein, so-called factor VIII related protein (16), which can be determined immunologically (VIII:R:AG, factor VIII related antigen). This protein resists proteolytic degradation better than VII1:C (13). A discrepancy between VII1:C and VII1:R:AG may thus indicate pathological proteolysis.…”
mentioning
confidence: 94%
“…The AHF activity may be low in some acquired diseases, such as osteomyelo- Penick 1957, Donaldsen 1960, Pasquini & Hershgold 1973, which may thus be reduced in fibrinolytic states (NilChn 1962). The AHF activity may also be low in intravascular coagulation (Merskey 1969, Ratnoff 1969, Lasch et a1 1971, Colman et a1 1972.…”
mentioning
confidence: 99%