Please use this identifier to cite or link to this item: http://hdl.handle.net/20.500.12779/4009
Title: Purification and biochemical characterization of calmodulin from Corylus avellana pollen
Authors: Scali, Monica
Cai, Giampiero
DEL CASINO, Cecilia
Santucci, Annalisa 
Tirlapur, U. K.
Moscatelli, A.
Cresti, Mauro
Tiezzi, A.
Issue Date: 1994
Project: None 
Journal: PLANT PHYSIOLOGY AND BIOCHEMISTRY
Abstract: 
A calcium-binding protein identifiable as calmodulin has been isolated from Corylus avellana L. pollen by phenyl-sepharose chromatography and further purified by anion exchange fast protein liquid chromatography. This protein is recognized by a monoclonal antibody raised against pea calmodulin. It can activate bovine brain phosphodiesterase in a calcium dependent manner and shows a calcium dependent shift in electrophoretic mobility. 2-D gel electrophoresis reveals that the polypeptide is present as a single isoform in Corylus pollen. In addition the amino acid sequence of this protein is largely comparable to that of other known plant calmodulins and to bovine brain calmodulin.
Description: 
53778
URI: http://hdl.handle.net/20.500.12779/4009
ISSN: 0981-9428
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