Immunoblotting and cytochemical characterization of human enamel proteins.
Mature enamel proteins (tuft proteins) and fetal enamel proteins were extracted by an homogenizing buffer method, subjected to SDS-PAGE and immunoblotted with a polyclonal antibody raised against the mature enamel proteins. Both fetal and tuft proteins were recognized by this immunoblotting. With the same antibody, immunolocalization of the developing enamel proteins was done on semi-thin-sections of human fetal tissue at the secretory stage, using an immunoperoxidase technique. Specific labelling of the enamel protein matrix was observed. It is concluded that a polyclonal antibody against mature enamel proteins (anti-tuft) can recognize the developing protein matrix at the secretory stage. This suggests that a common antigenic determinant is maintained throughout the course of amelogenesis in human enamel.
Farge
P
P
Faculté d'Odontologie, URA CNRS 244, Université Claude Bernard, Lyon, France.
Ricard-Blum
S
S
Joffre
A
A
Ville
G
G
Magloire
H
H
D000328:Adult; D000565:Ameloblasts / Q000737:chemistry / Q000473:pathology; D003746:Dental Enamel Proteins / Q000032:analysis*; D004591:Electrophoresis, Polyacrylamide Gel; D004658:Enamel Organ / Q000737:chemistry / Q000473:pathology; D005326:Fetal Proteins / Q000032:analysis; D005333:Fetus; D006651:Histocytochemistry; D006801:Humans; D015151:Immunoblotting; D008970:Molecular Weight; D012967:Sodium Dodecyl Sulfate
D003746:Dental Enamel Proteins; D005326:Fetal Proteins; D012967:Sodium Dodecyl Sulfate