Organization of the human alpha 2-plasmin inhibitor gene.
نویسندگان
چکیده
منابع مشابه
Synthesis and secretion of alpha 2-plasmin inhibitor by established human liver cell lines.
The site of synthesis of alpha 2-plasmin inhibitor (alpha 2-PI), a physiologic inhibitor of plasmin, is not known with certainty. We have studied the production and secretion of alpha 2-PI by three established human liver cell lines derived from hepatocellular carcinoma and hepatoblastoma (Hep G2, Hep 3B, and PLC/PRF/5). As measured by a specific radioimmunoassay, the titer of alpha 2-PI increa...
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Purified al-proteolytic inhibitor from human plasma was shown to inhibit trypsin, chymotrypsin, plasmin, and thrombin. This inhibitor is probably identical with the inhibitor previously known as serum trypsin inhibitor, al-antitrypsin, or antiplasmin. The enzymes were affected by the inhibitor via two different mechanisms. Trypsin and chymotrypsin reacted instantaneously in stoichiometric manne...
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When blood plasma containing the NH2-terminal 12-residue peptide (N-peptide) of alpha 2-plasmin inhibitor (alpha 2PI; alpha 2-antiplasmin) was clotted in the presence of calcium ions, the N-peptide and alpha 2PI were cross-linked to fibrin by activated coagulation factor XIII. The amount of N-peptide cross-linked to fibrin was proportional to the concentration of N-peptide present in plasma. On...
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An enzyme-linked immunosorbent assay (ELISA) has been developed for the quantification of alpha 1-antitrypsin-human leukocyte elastase (alpha 1AT-E) complexes. In the ELISA, the alpha 1AT-E complex is bound to a surface by rabbit antileukocyte elastase antibody, and the inhibitor-proteinase complex is quantified by a second antibody, rabbit anti-alpha 1-antitrypsin F(ab')2, labeled with alkalin...
متن کاملKinetics of plasmin inhibition in the presence of a synthetic tripeptide substrate. The reaction with pancreatic trypsin inhibitor and two forms of alpha 2-plasmin inhibitor.
The progressive inhibition of plasmin by pancreatic trypsin inhibitor and by alpha 2-plasmin inhibitor in the presence of D-valyl-L-leucyl-L-lysine 4-nitroanilide was investigated. The kinetics with plasmin were compared with those with miniplasmin. The kinetic properties of two functionally different forms of alpha 2-plasmin inhibitor described by Clemmensen [(1979) in The Physiological Inhibi...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1988
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.85.18.6836