RESUMO
Extremely acidic copper-containing proteins, neurocupreins, were isolated from brains of various mammals (bovine, rabbit, pig and sheep). Neurocupreins from all these sources were found to have similar physico-chemical and antigenic properties. Using the immunological approach, it was shown that neurocuprein is located only in brain cytosol and synaptosomal fractions. Extremely acidic copper-containing proteins were also isolated from soluble and membranous fractions of chromaffin granules from bovine adrenal medulla. The soluble form of the protein from the granules has practically the same physico-chemical and antigenic properties as neurocupreins. The copper protein isolated from membranes of granules has slightly higher molecular weight and somewhat different amino acid composition, although their EPR spectra are identical. However, both copper proteins from chromaffin granules are immunoprecipitated with antibodies to neurocuprein. It is suggested that the membranous form differs from the soluble one in possessing a peptide which prolongs the protein chain without changes in its antigenic properties.
Assuntos
Antígenos/isolamento & purificação , Química Encefálica , Grânulos Cromafim/análise , Sistema Cromafim/análise , Metaloproteínas/isolamento & purificação , Animais , Bovinos , Fenômenos Químicos , Físico-Química , Cromatografia em Gel , Espectroscopia de Ressonância de Spin Eletrônica , Imunoquímica , Proteínas de Membrana/isolamento & purificação , Coelhos , Ovinos , Frações Subcelulares/análise , SuínosAssuntos
Medula Suprarrenal/análise , Grânulos Cromafim/análise , Sistema Cromafim/análise , Proteínas do Tecido Nervoso/isolamento & purificação , Aminoácidos/análise , Animais , Bovinos , Cobre/análise , Dopamina beta-Hidroxilase/análise , Espectroscopia de Ressonância de Spin Eletrônica , Epinefrina , Peso Molecular , OxirreduçãoRESUMO
The incubation of adrenal ferredoxin with various detergents in the presence of oxygen or ferricyanide leads to bleaching of the protein. The bleached preparation has the properties of apoferredoxin and it can be reconstituted with high yield by conventional methods.
