Isolation and characterization of a calmodulin-like protein from the cyanobacterium Nostoc sp. PCC 6720 |
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Authors: | Leonzio A Onek Peter J Lea R John Smith |
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Institution: | (1) Institute of Environmental and Biological Sciences, Division of Biological Sciences, Lancaster University, LA1 4YQ Lancaster, UK |
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Abstract: | A 21-kDa novel polypeptide which possesses characteristics normally considered to be diagnostic of the calmodulin present in eukaryotic cells was isolated from the cyanobacterium Nostoc sp. PCC 6720. The major technique employed in the isolation of the polypeptide was ion-exchange chromatography on a Mono Q column. The 21-kDa polypeptide was shown: to activate pea NAD kinase in vitro, in a Ca2+ requiring reaction; to react with polyclonal antibodies raised against spinach calmodulin, but not with those raised against bovine brain calmodulin; and to exhibit a Ca2+ dependent shift in migration during SDS-PAGE.Abbreviations ATCC
American Type Culture Collection
- DCPIP
2,6-dichlorophenylindophenol
- PBS
Phosphate buffered saline |
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Keywords: | Calcium binding protein Calmodulin Nostoc sp PCC 6720 |
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