Abstract:
:Bordetella calmodulin-like protein was purified from culture supernatant fluid of B. pertussis, B. parapertussis and B. bronchiseptica by successive chromatography on hydroxyapatite, Toyopearl HW-50F and QAE-Toyopearl 550C columns. The purified calmodulin-like protein appeared to be homogeneous by SDS-polyacrylamide gel electrophoresis. The apparent molecular mass of calmodulin-like protein on SDS-polyacrylamide gel electrophoresis was 10 kDa, which was smaller than bovine brain calmodulin (17 kDa). The purified calmodulin-like protein activated both Bordetella adenylate cyclase and mammalian phosphodiesterase in a Ca(2+)-dependent manner. This activation was inhibited by calmodulin antagonists. The calmodulin-like protein, like calmodulin, was retained by a hydrophobic resin in the presence of Ca2+ and eluted by the addition of EDTA. These results indicated that the Bordetella calmodulin-like protein is closely related to calmodulin. As a putative calmodulin the extracellular calmodulin may be involved in Bordetella pathogenesis.
journal_name
FEMS Microbiol Lettjournal_title
FEMS microbiology lettersauthors
Nagai M,Endoh M,Danbara H,Nakase Ydoi
10.1111/j.1574-6968.1994.tb06696.xsubject
Has Abstractpub_date
1994-02-15 00:00:00pages
169-74issue
2eissn
0378-1097issn
1574-6968journal_volume
116pub_type
杂志文章abstract::The devR-devS two-component system of Mycobacterium tuberculosis was identified earlier and partially characterized in our laboratory. A devR::kan mutant of M. tuberculosis was constructed by allelic exchange. The devR mutant strain showed reduced cell-to-cell adherence in comparison to the parental strain in laborato...
journal_title:FEMS microbiology letters
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journal_title:FEMS microbiology letters
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journal_title:FEMS microbiology letters
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journal_title:FEMS microbiology letters
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pub_type: 杂志文章
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