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

Links

Text available via DOI:

View graph of relations

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

Research output: Contribution to journalJournal article

Published
Close
<mark>Journal publication date</mark>1994
<mark>Journal</mark>Archives of Microbiology
Issue number4
Volume161
Number of pages7
Pages (from-to)352-358
<mark>State</mark>Published
<mark>Original language</mark>English

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.