The dimerization of half-molecule fragments of transferrin.
Partial proteolysis was used to prepare half-molecule fragments of hen ovotransferrin. N-Terminal and C-terminal fragments associate to form an N-terminal fragment-C-terminal fragment dimer. Variant forms of the N- and C-terminal fragments can be prepared in which a few amino acid residues are lacking from the C-terminal ends of the fragments. These variant fragments are partially or completely unable to associate; the suggestion that the molecular recognition sites are located in these C-terminal stretches of the N-terminal half-molecule (320-332) and of the C-terminal half-molecule (683-686) is in agreement with X-ray-crystallography data for human lactotransferrin [Anderson, Baker, Dodson, Norris, Rumball, Waters & Baker (1987) Proc. Natl. Acad. Sci. U.S.A. 84, 1769-1773].
Department of Biochemistry, University of Bristol, U.K.
J
J
Williams
K
K
Moreton
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D001704:Biopolymers; D043424:Carboxypeptidase B; D002268:Carboxypeptidases; D002645:Chickens; D002850:Chromatography, Gel; D003207:Conalbumin; D004372:Ducks; D004527:Egg Proteins; D007501:Iron; D008722:Methods; D008969:Molecular Sequence Data; D010446:Peptide Fragments; D011485:Protein Binding / Q000187:drug effects; D011784:Quail; D012492:Salts; D013820:Thermolysin; D014357:Trypsin
D001704:Biopolymers; D004527:Egg Proteins; D010446:Peptide Fragments; D012492:Salts; D003207:Conalbumin; D007501:Iron; D002268:Carboxypeptidases; D043424:Carboxypeptidase B; D014357:Trypsin; D013820:Thermolysin