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 bin...

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Bibliographic Details
Published in:Biochemical journal 1992-08, Vol.285 (3), p.711-714
Main Authors: KUBAL, G, MASON, A. B, SADLER, P. J, TUCKER, A, WOODWORTH, R. C
Format: Article
Language:English
Subjects:
Aluminum - metabolism
Amino Acid Sequence
Analytical, structural and metabolic biochemistry
Apoproteins - chemistry
Apoproteins - metabolism
Binding Sites
Biological and medical sciences
Fundamental and applied biological sciences. Psychology
Humans
Hydrogen-Ion Concentration
Magnetic Resonance Spectroscopy
Metalloproteins
Models, Molecular
Molecular Sequence Data
Molecular Structure
Other metalloproteins
Proteins
Recombinant Proteins - chemistry
Recombinant Proteins - metabolism
Transferrin - chemistry
Transferrin - metabolism
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Summary: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.
ISSN:0264-6021
1470-8728
DOI:10.1042/bj2850711