| Literature DB >> 1497609 |
G Kubal1, A B Mason, P J Sadler, A Tucker, R C Woodworth.
Abstract
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.Entities:
Mesh:
Substances:
Year: 1992 PMID: 1497609 PMCID: PMC1132852 DOI: 10.1042/bj2850711
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857