Literature DB >> 2438803

Monoclonal antibodies directed against human tissue-type plasminogen activator: a characterization of their species specificity, affinity and heavy-chain binding.

J F Cajot, E Bachmann, E Cousin, E K Kruithof, W D Schleuning, J Hauert, F Bachmann.   

Abstract

Six monoclonal antibodies (mIgG) and a polyclonal antibody (pIgG) directed against human tissue-type plasminogen activator (t-PA) were tested for their species specificity towards human or murine t-PA. Whereas pIgG as well as several mIgGs discriminated poorly between these two t-PA species, one mIgG (clone E3) was highly specific for human t-PA. Inhibition and binding studies of human t-PA by mIgGs revealed high affinity-high inhibitory (E3) as well as high affinity-poor inhibitory (B1) mIgGs. The relative affinity of two mIgGs for human t-PA was found to be equal or even superior to that of pIgG. Immunoblotting of reduced two-chain t-PA and of an isolated heavy chain of t-PA prepared by recombinant DNA technology, showed that the E3 antibody was directed against the heavy chain of t-PA.

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Year:  1987        PMID: 2438803     DOI: 10.1016/0049-3848(87)90214-3

Source DB:  PubMed          Journal:  Thromb Res        ISSN: 0049-3848            Impact factor:   3.944


  1 in total

1.  Characterization of the binding of plasminogen activators to plasma membranes from human liver.

Authors:  G Nguyen; S J Self; C Camani; E K Kruithof
Journal:  Biochem J       Date:  1992-11-01       Impact factor: 3.857

  1 in total

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