Cr(TREN)–ferritin Interactions. (A) The effect of
ferritin on the Cr(TREN) spectrum. UV-vis spectra showing the shift in
the Cr(TREN) d-d bands on complexation to rH-L134P, with two apparent
isosbestic points at 544 and 460 nm. Cr(TREN) (0.4 mM, 2 equivalents
per subunit) was incubated with rH-L134P (8 μM) at 25°C. Spectra
were taken at 20-min intervals. The absorption spectrum of the protein
in buffer, before Cr(TREN) addition, was used as a reference.
(B) The effect of Cr(TREN) on protein surface charge
(electrophoretic mobility). Migration of rH-L134P, with varying amounts
of bound Cr(TREN) during electrophoresis in native polyacrylamide gels
(6%). Values shown are Cr(TREN) per subunit after removing unbound
Cr(TREN) by dialysis.