Literature DB >> 1955855

Purification and some characteristics of a calcium-binding protein from Bacillus cereus spores.

Y T Shyu1, P M Foegeding.   

Abstract

A novel calcium-binding protein has been purified from the dormant spores of Bacillus cereus T. Purity of this protein was verified by SDS-PAGE and reversed-phase HPLC. Its calcium-binding ability was verified by a competitive calcium-binding assay using Chelex-100 resin and 45Ca autoradiography. The protein is heat-stable and is retained by hydrophobic matrices (phenyl-Sepharose) in a calcium-dependent manner. SDS-PAGE and amino acid composition indicate the molecular mass of the protein to be 24 kDa.

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Year:  1991        PMID： 1955855     DOI： 10.1099/00221287-137-7-1619

Source DB:  PubMed          Journal:  J Gen Microbiol        ISSN： 0022-1287


  3 in total

1.  Isolation and characterization of a calmodulin-like protein from Halobacterium salinarium.

Authors:  T Rothärmel; G Wagner
Journal:  J Bacteriol       Date:  1995-02       Impact factor: 3.490

2.  Immunocytochemical localization of a calmodulinlike protein in Bacillus subtilis cells.

Authors:  D C Dominguez; H Adams; J H Hageman
Journal:  J Bacteriol       Date:  1999-08       Impact factor: 3.490

3.  Cloning and expression of the gene for a novel protein from Mycobacterium smegmatis with functional similarity to eukaryotic calmodulin.

Authors:  Prasad T Reddy; C Rama Prasad; P Hemalatha Reddy; Dennis Reeder; Keith McKenney; Howard Jaffe; Mariana N Dimitrova; Ann Ginsburg; Alan Peterkofsky; P Suryanarayana Murthy
Journal:  J Bacteriol       Date:  2003-09       Impact factor: 3.490
  3 in total

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