Uptake of Al3+ into the N-lobe of human serum transferrin.
We have studied the binding of Al3+ to human serum apotransferrin (80 kDa) and recombinant N-lobe human apotransferrin (40 kDa) in 0.1 M-sodium bicarbonate solution at a pH meter reading in 2H2O (pH*) of 8.8 using 1H n.m.r. spectroscopy. The results show that for the intact protein, preferential binding of Al3+ to the N-lobe occurs. Molecular modelling combined with an analysis of ring-current-induced shifts suggest that n.m.r. spectroscopy can be used to probe hinge bending processes which accompany metal uptake in solution.
Kubal
G
G
Department of Chemistry, Birkbeck College, University of London, U.K.
Mason
A B
AB
Sadler
P J
PJ
Tucker
A
A
Woodworth
R C
RC
D000535:Aluminum / Q000378:metabolism*; D000595:Amino Acid Sequence; D001059:Apoproteins / Q000737:chemistry / Q000378:metabolism*; D001665:Binding Sites; D006801:Humans; D006863:Hydrogen-Ion Concentration; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D008969:Molecular Sequence Data; D015394:Molecular Structure; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D014168:Transferrin / Q000737:chemistry / Q000378:metabolism*
D001059:Apoproteins; D011994:Recombinant Proteins; D014168:Transferrin; C028284:apotransferrin; D000535:Aluminum