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. 1975 Jul;72(7):2577–2581. doi: 10.1073/pnas.72.7.2577

Amino-acid sequence of activation cleavage site in plasminogen: homology with "pro" part of prothrombin.

L Sottrup-Jensen, M Zajdel, H Claeys, T E Petersen, S Magnusson
PMCID: PMC432812  PMID: 1058475

Abstract

A 38-residue fragment is isolated from carboxymethylated plasminogen. Residues 29-38 have the same sequence as the amino-terminal end of the light chain of plasmin. The sequence 1-28 is therefore the sequence of the carboxyl-terminal end of the heavy chain and contains the specific sequence at which urokinase (EC 3.4.99.26) and other plasminogen-activating serine proteases split. Two of the five carboxymethyl-cysteine residues in the isolated fragment are situated close to the cleavage site and the fragment is not itself a substrate for plasminogen-activators. Residues 1-11 show extensive sequence homology with residues 137-147 and 242-252 in prothrombin, which are located in corresponding regions of the two internally homologous 83-residue structures in the non-thrombin part of the molecule, indicating that such structures may be a common feature of the non-protease part of the larger serine protease zymogens.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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