Purification and characterization of Bordetella calmodulin-like protein.

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 Lett

authors

Nagai M,Endoh M,Danbara H,Nakase Y

doi

10.1111/j.1574-6968.1994.tb06696.x

subject

Has Abstract

pub_date

1994-02-15 00:00:00

pages

169-74

issue

2

eissn

0378-1097

issn

1574-6968

journal_volume

116

pub_type

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