Title : Proteolytically cleaved mutant antithrombin-Hamilton has high stability to denaturation characteristic of wild type inhibitor serpins.

Pub. Date : 1994 Jul 4

PMID : 8026575






2 Functional Relationships(s)
Download
Sentence
Compound Name
Protein Name
Organism
1 We have measured the stability to denaturation of one of these non-inhibitor substrate mutants, antithrombin-Hamilton, which has an Ala-->Thr change at position P12 in strand s4A. Alanine serpin family C member 1 Homo sapiens
2 We find that it undergoes the transformation to the more stable form which is observed for inhibitor serpins, from which we conclude that the Ala-->Thr change in antithrombin-Hamilton does not prevent insertion of s4A into beta-sheet A in the cleaved form. Alanine serpin family C member 1 Homo sapiens