Production and characterization of an anti-chicken transferrin.
Several lines of recent evidence have suggested that transferrin plays a significant role in tissue interaction or morphogenesis at early stages of embryo development. In the present study, an anti-chicken transferrin antibody was produced and its basic characteristics were clarified as a basis for use in further studies. An antiserum termed Toraji 3 was raised against chicken transferrin and purified into IgG and ligand-affinity-purified fractions. These three preparations of the antibody gave an intense immunohistochemical signal in visceral yolk sac and developing liver, both of which are known to be major producers of transferrin in early development. In immunoblot analysis, these three preparations detected 70-kDa transferrin, whereas the ligand-affinity-purified preparation showed higher specificity. It was also demonstrated by enzyme-linked immunosorbent assay and immunoblotting that Toraji 3 antibody bound preferentially to chicken transferrin and showed a negligible binding to human transferrin.
Shimizu
O
O
Department of Oral and Maxillofacial Surgery, Nihon University School of Dentistry, Tokyo, Japan.
Isokawa
K
K
Kanematsu
K
K
Ohtsu
J
J
Iwata
T
T
Matsui
H
H
Sato
H
H
Toda
Y
Y
D000818:Animals; D000918:Antibody Specificity / Q000276:immunology; D002642:Chick Embryo; D006801:Humans; D007074:Immunoglobulin G / Q000096:biosynthesis*; D008024:Ligands; D014168:Transferrin / Q000276:immunology*
D007074:Immunoglobulin G; D008024:Ligands; D014168:Transferrin