Purification and some characteristics of a calcium-binding protein from Bacillus cereus spores.
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.
Shyu
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Department of Food Science, North Carolina State University, Raleigh 27695-7624.
Foegeding
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D000596:Amino Acids / Q000032:analysis; D001409:Bacillus cereus / Q000737:chemistry* / Q000502:physiology; D002118:Calcium / Q000378:metabolism; D002135:Calcium-Binding Proteins / Q000737:chemistry / Q000302:isolation & purification*; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D013171:Spores, Bacterial / Q000737:chemistry*; D013696:Temperature
D000596:Amino Acids; D002135:Calcium-Binding Proteins; D002118:Calcium