Identification of parvalbumin alpha in bovine hypothalamus: a partial primary structure.
Neurochem Res
; 22(7): 799-803, 1997 Jul.
Article
em En
| MEDLINE
| ID: mdl-9232631
ABSTRACT
In the course of the study of structure-functional properties and molecular mechanisms of neuropeptides and of low molecular weight proteins of the central nervous system we succeeded in isolating from the soluble fraction of bovine hypothalamus a protein having M(r) 11897.3, according to mass spectral analysis. The purification procedure was mainly based on reversed phase HPLC. As the N-terminus of the molecule was found to be blocked, we have subjected it to CNBr degradation. By Edman microsequence analysis of the peptide fragments and by data base searching the isolated substance was identified as parvalbumin alpha (PRVA)-one of the calcium-binding proteins. However, its primary structure was found not to be identical to that of the known PRVAs from other sources. One of the features of PRVA is its stability. Being subjected to an exhausting purification procedure it retains its complete structure. As neuropeptides and low molecular weight proteins are found to be polyfunctional, a central question concerns the biological role of PRVAs in terms of "where and when" they express their action.
Buscar no Google
Base de dados:
MEDLINE
Assunto principal:
Parvalbuminas
/
Proteínas de Ligação ao Cálcio
/
Hipotálamo
/
Proteínas do Tecido Nervoso
Tipo de estudo:
Diagnostic_studies
Idioma:
En
Revista:
Neurochem Res
Ano de publicação:
1997
Tipo de documento:
Article
País de afiliação:
Federação Russa