Abstract:
:The gene of ecotin, an E. coli proteinase inhibitor, was cloned, and by site-directed mutagenesis the active site residue of the protein, Met84, was mutated to Lys, Arg and Leu. The recombinant wild-type and mutant inhibitors were overexpressed in E. coli, purified to homogeneity and their inhibitory effects on trypsin, chymotrypsin and elastase were compared. Of these serine proteinases trypsin is the most strongly inhibited by wild type ecotin and its mutants. According to our results the character of residue 84 of ecotin significantly but not dramatically modifies the specificity of the inhibitor.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Pál G,Sprengel G,Patthy A,Gráf Ldoi
10.1016/0014-5793(94)80584-9subject
Has Abstractpub_date
1994-03-28 00:00:00pages
57-60issue
1eissn
0014-5793issn
1873-3468pii
0014-5793(94)80584-9journal_volume
342pub_type
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