Human placental ferritin receptor.
Biochim Biophys Acta
; 884(1): 31-8, 1986 Oct 29.
Article
em En
| MEDLINE
| ID: mdl-3021231
ABSTRACT
Brush-border membranes from human placenta were prepared and their purity was clarified by biochemical and morphological methods. Ferritin binding to these prepared membranes was examined using horse spleen 125I-apoferritin, and was found to be completed within 10 min at 37 degrees C and pH 7.5. The amount of ferritin bound to the membranes was found to be proportional to the amount of membrane added and saturable for a given amount of the membrane in the presence of excess ligand. The membranes exhibited specific ferritin binding with a Ka of 2.3 X 10(7) M-1 at pH 7.5. A competitive binding assay indicated that horse spleen 125I-apoferritin binding was inhibited by a 10-fold molar excess of horse spleen ferric ferritin and a 500-fold molar excess of human transferrin. These results suggest that human placental brush-border membranes have specific receptors for horse spleen apoferritin molecules.
Buscar no Google
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Placenta
/
Receptores de Superfície Celular
/
Proteínas de Ligação ao Ferro
Limite:
Female
/
Humans
/
Pregnancy
Idioma:
En
Revista:
Biochim Biophys Acta
Ano de publicação:
1986
Tipo de documento:
Article