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Fucoidan alginate and sulfated alginate microbeads induce distinct coagulation, inflammatory and fibrotic responses. [PDF]
Vasuthas K+8 more
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Acute obstetric coagulopathy: need for innovation. [PDF]
Chumappumkal Joseph B, von Drygalski A.
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Plasmin-α2-antiplasmin complexes (plasmin—plasmin inhibitor complexes) [PDF]
α2-Antiplasmin (new name: plasmin inhibitor) is the most important plasmin inhibitor. Its rapid reaction with plasmin results in the formation of an inactive complex composed of one molecule of each component. Two steps are involved in this process: first a reversible complex is formed between the lysine-binding sites of plasmin and complementary sites
E. Hattey+4 more
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Thrombosis Research, 1993
In order to understand the mechanism for the complex between alpha 2-plasmin-inhibitor (alpha 2-PI) and plasmin to express its specific activity on fibrin autography after SDS-PAGE, we analyzed the effects of SDS on alpha 2-PI molecule and alpha 2-PI-plasmin complex.
Tetsumei Urano+3 more
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In order to understand the mechanism for the complex between alpha 2-plasmin-inhibitor (alpha 2-PI) and plasmin to express its specific activity on fibrin autography after SDS-PAGE, we analyzed the effects of SDS on alpha 2-PI molecule and alpha 2-PI-plasmin complex.
Tetsumei Urano+3 more
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Plasmin-α2-plasmin inhibitor complex and α2-plasmin inhibitor in chronic subdural hematoma
Journal of Neurosurgery, 1989✓ Levels of the plasmin-α2-plasmin inhibitor complex (PLN-A2PI complex) and α2-plasmin inhibitor (A2PI) were determined by enzyme-linked immunosorbent assay (ELISA) with monoclonal antibodies in 59 patients with 66 chronic subdural hematomas (SDH's). Normal concentrations of the PLN-A2PI complex and A2PI in plasma are below 0.8 µg/ml and 60.5 ± 16.1 µg/
Kenichi Saito+3 more
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1976
Publisher Summary Plasmin is a serine protase with trypsin-like specificity. It cleaves or hydrolyzes proteins and peptides at arginyl and lysyl peptide bonds, and basic amino acid esters, and amides. Plasmin appears to have a preference for lysyl bonds in both protein and ester substrates.
Kenneth C. Robbins, Louis Summaria
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Publisher Summary Plasmin is a serine protase with trypsin-like specificity. It cleaves or hydrolyzes proteins and peptides at arginyl and lysyl peptide bonds, and basic amino acid esters, and amides. Plasmin appears to have a preference for lysyl bonds in both protein and ester substrates.
Kenneth C. Robbins, Louis Summaria
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Plasmin inactivation in Plasma
Thrombosis and Haemostasis, 1976SummaryInhibition and inactivation of plasmin is ascribed to α2-macroglobulin, α1-antitrypsin and c1-esterase inhibitor. In an “overall” inactivation test of plasmin in plasma, which comes perhaps closest to rapid inactivation of plasmin in the circulating blood, we only found a correlation between the immunological concentration of α2-macroglobulin ...
Vreeken J, E. M Haselager, Th. M Goote
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Fragmentation of Haptoglobin by Plasmin
Canadian Journal of Biochemistry, 1971Human haptoglobin type Hp 1-1, is hydrolyzed by plasmin to give two dissimilar products, P1 and P2, with molecular weights of 78 000 and 17 000, respectively. The larger fragment, P1 has the same N-terminal amino acids, valine and isoleucine, as intact haptoglobin.
Frederick A. Ofosu+2 more
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Thrombosis and Haemostasis, 1975
SummaryAn international collaborative study involving ten laboratories was undertaken to assess the suitability of a preparation of human plasmin in 50% glycerol to serve as a single standard for the bioassay of plasmin activity. The study included examination of the stability of the proposed standard and comparisons between assay methods.
P. J Campbell+2 more
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SummaryAn international collaborative study involving ten laboratories was undertaken to assess the suitability of a preparation of human plasmin in 50% glycerol to serve as a single standard for the bioassay of plasmin activity. The study included examination of the stability of the proposed standard and comparisons between assay methods.
P. J Campbell+2 more
openaire +3 more sources