Immunological characterization and phosphorylation of a novel cardiac calmodulin-binding protein
Proceedings of the Caribbean Academy of Sciences
; 3: 72-77, 1992. ilus, tab
Article
em En
| MedCarib
| ID: med-2510
Biblioteca responsável:
JM3.1
Localização: JM9.1; Q29.C372 1992
ABSTRACT
Calmodulin is an ubiquitous, malfunctional 17kDa, acidic protein which is activated by Ca2+ and regualates the function of many enzymes and other cellular proteins. A novel bovine heart high molecular weight Ca2+ /Calmodulin-binding protein was recently reported by Sharma (J.Biol. Chem. 265, 1152-1157, 1990) and Barnes and Sharma (Faseb J. 5 449, 1991). In this work, we have investigated the distribution of this 175 kDA protein (Mr 140 000) in various bovine tissues. The polyclonal antibody to the protein was used to show its presence in the heart, lung, brain and pancreas but not in spleen, Kidney, uterus and skeletal muscles. The protein was phosphorylated by a novel endogenous protein kinase with a stoichiometry of 1 mole of phosphate incorporated per mole of protein in a Ca2+ /Calmodulin-dependant manner(AU)
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Coleções:
01-internacional
Base de dados:
MedCarib
Assunto principal:
Fosforilação
/
Proteínas de Ligação a Calmodulina
Idioma:
En
Revista:
Proceedings of the Caribbean Academy of Sciences
Ano de publicação:
1992
Tipo de documento:
Article