title: Purification and characterization of ferritin from alfalfa seeds.
abstract: Ferritin from alfalfa (Medicago sativa) seeds was isolated, purified, and characterized. The apparent molecular mass of the native protein was found to be 560 kDa. Electrophoresis in denaturing gradient polyacrylamide-SDS gels revealed subunits of 28-26.5 kDa. The average iron cores were 4 nm in diameter and contained about 1400 iron atoms, with an iron-to-phosphorus ratio of 4:1. N-terminal amino acid sequencing of the 28 kDa subunit revealed close homology with other plant proteins. Immunochemical analysis using polyclonal antibodies raised against pea-seed ferritin has confirmed, in agreement with previous reports, that plant proteins share common epitopes.
authors.affiliation: Departamento de Biología Fundamental y Ciencias de la Salud, Universidad de las Islas Baleares, Palma de Mallorca, Spain.
authors.forename: F
authors.initials: F
authors.lastname: Barceló
authors.forename: F
authors.initials: F
authors.lastname: Miralles
authors.forename: C
authors.initials: C
authors.lastname: Otero Areán
mesh_terms: D000595:Amino Acid Sequence; D005293:Ferritins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification*; D000455:Medicago sativa / Q000737:chemistry* / Q000235:genetics; D008854:Microscopy, Electron; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010940:Plant Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification*; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid
chemical_list: D010940:Plant Proteins; D005293:Ferritins