We have over 12,000 students, from over 100 countries, within one of the safest campuses in the UK


97% of Lancaster students go into work or further study within six months of graduating

Home > Research > Publications & Outputs > Isolation and characterization of a calmodulin-...
View graph of relations

« Back

Isolation and characterization of a calmodulin-like protein from the cyanobacterium Nostoc sp. PCC 6720.

Research output: Contribution to journalJournal article


<mark>Journal publication date</mark>1994
<mark>Journal</mark>Archives of Microbiology
Number of pages7
<mark>Original language</mark>English


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.