[Preparation, characterization and receptor-binding capacity of pig serum transferrin half-molecules containing a single iron-binding site].
N- and C-half molecules containing a single iron-binding site were simultaneously obtained from trypsin digest of iron-saturated pig transferrin. The activities of the pig serum transferrin and of its N- and C-half molecules to bind the human placental membrane transferrin receptor were compared. The results indicate that the receptor-binding site of pig transferrin may be located at the C-half molecule of the transferrin.
Zhang
Xin-Tang
XT
State Key Laboratory of Molecular Biology, Shanghai Institute of Biochemistry, Shanghai 200031, China.
Tang
Yue-Hua
YH
Feng
You-Min
YM
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001667:Binding, Competitive; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D006801:Humans; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism; D011990:Receptors, Transferrin / Q000378:metabolism*; D013552:Swine; D014168:Transferrin / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*
D000596:Amino Acids; D010446:Peptide Fragments; D011990:Receptors, Transferrin; D014168:Transferrin