Open AccessInactivation of the streptokinase gene prevents Streptococcus equisimilis H46A from acquiring cell‐associated plasmin activity in the presence of plasminogen
Author(s) -
Malke Horst,
Mechold Undine,
Gase Klaus,
Gerlach Dieter
Publication year - 1994
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1994.tb06683.x
Subject(s) - plasmin , streptokinase , zymogen , chemistry , biochemistry , mutant , microbiology and biotechnology , mutagenesis , receptor , gene , enzyme , biology , medicine , psychiatry , myocardial infarction
The streptokinase gene of Streptococcus equisimilis H46 was inactivated by plasmid insertion mutagenesis to study the relationship between elaboration of streptokinase and acquisition of cell‐associated plasmin activity after incubation of wild‐type and mutant cells in media containing plasminogen or plasmin. The results showed that H46A binds both the zymogen and active enzyme, generates surface‐associated plasmin activity in the presence of plasminogen when producing streptokinase, and expresses its plasmin(ogen) receptor(s) independently of a functional streptokinase gene. At least part of the plasmin(ogen) binding capacity may be due to the glyceraldehyde‐3‐phosphate dehydrogenase type of receptor molecule, as judged by the detection of the corresponding gene.