Characterization and immunological analysis of ferritin from the hemolymph of Galleria mellonella.
Comp Biochem Physiol A Mol Integr Physiol
; 129(2-3): 501-9, 2001 Jun.
Article
de En
| MEDLINE
| ID: mdl-11423320
ABSTRACT
Ferritin, an iron-binding protein, was purified from the larval hemolymph of the wax moth, Galleria mellonella by KBr density ultracentrifugation and FPLC (Superose 6). The iron content of ferritin was determined by atomic emission spectroscopy and Ferene S stain. Native molecular mass of ferritin was estimated as 630 kDa. SDS-PAGE revealed that the ferritin consists of two major polypeptides of 26 and 32 kDa and one minor polypeptide of 30 kDa. An isoelectric point of ferritin was measured to be approximately 7.3 and only the 32-kDa subunit is glycosylated. The ferritin contains large amounts of lysine, glutamine, glutamic acid and leucine but tryptophan was not detected. Electron microscopic examination of negatively stained preparations showed an 11-nm particle in external diameter and 7-nm iron core. Ferritin is present in both the ovary and testis. Localization of ferritin by immunoelectron microscopy in ovary and testis revealed that the gold particles were located in vitelline membrane and yolk granules but not in follicular epithelium of ovary. In the testis, the gold particles were located in testicular fluid and lumen of vas deferens.
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Collection:
01-internacional
Base de données:
MEDLINE
Sujet principal:
Hémolymphe
/
Ferritines
/
Papillons de nuit
Limites:
Animals
Langue:
En
Journal:
Comp Biochem Physiol A Mol Integr Physiol
Sujet du journal:
BIOLOGIA MOLECULAR
/
FISIOLOGIA
Année:
2001
Type de document:
Article
Pays d'affiliation:
Corée du Sud