ArticleFish physiology and biochemistry2009
Purification and characterization of alpha(1)-proteinase inhibitor and antithrombin III: major serpins of rainbow trout (Oncorhynchuss mykiss) and carp (Cyprinus carpio) blood plasma.
Article in Fish physiology and biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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2 citing papers in PubMed, 7 citations in OpenAlex.
- Proteomic profiling of the serological response to a chemically-inactivated nodavirus vaccine in European sea bass Dicentrarchus labrax.Veterinary research communications · 2025Article
- Amblyomma americanum tick saliva serine protease inhibitor 6 is a cross-class inhibitor of serine proteases and papain-like cysteine proteases that delays plasma clotting and inhibits platelet aggregation.Insect molecular biology · 2013Article
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1 author at 1 institution in 1 country.
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Abstract
The main serine proteinase inhibitors of rainbow trout (Oncorhynchuss mykiss) and common carp (Cyprinus carpio) blood plasma were isolated and purified. The investigated inhibitors, alpha(1)-proteinase inhibitor (alpha(1)-PI) and antithrombin III (AT III), act by forming stable complexes with target proteinases. The association rate constants k (on) for the interaction of fish plasma inhibitors with several serine proteinases have been determined: k (on) for both carp and rainbow trout alpha(1)-PI were >10(7) M(-1) s(-1) for human neutrophil elastase, and in the case of bovine trypsin and chymotrypsin k (on) values were 2.0-5.2 x 10(6) M(-1) s(-1). Association rate constants k (on) for the interaction of carp and rainbow trout AT III with bovine trypsin and thrombin were about 1.3 x 10(4)-7.9 x 10(5) M(-1) s(-1) without and >10(7) M(-1) s(-1) in presence of heparin; so antithrombins require the presence of heparin to become effective proteinase inhibitors. The high degree of homology of the estimated amino acid sequences of fish inhibitors reactive site loops confirms their similarity with other proteinase inhibitors from the serpin family.
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