. Author manuscript; available in PMC: 2011 Aug 1.

Published in final edited form as: Biochim Biophys Acta. 2010 Mar 20;1800(8):858–870. doi: 10.1016/j.bbagen.2010.03.012

Table 1.

Sedimentation parameters for horse spleen and human H-chain ferritins.^a

Protein	M (g/mol)	s_20,w (10⁻¹³s)	D_20,w (10⁻⁷cm²/s)	d (nm)
apoHoSF (monomer)^b	484,120	17.0 (0.6)	3.21 (0.15)	13.3
apoHoSF (dimer)^c	968,240	25.1 (0.1)	2.37 (0.10)	18.0
apoHuHF (monomer)^d	506,266	18.3 (0.1)	3.18 (0.09)	13.5
apoHuHF (dimer)^d	1,012,532	26.4 (0.2)	2.29 (0.20)	18.7

Estimated errors in parentheses.

Chemically prepared apoHoSF. Fractionated native HoSF (fraction # 1 of Fig. 9) gave s_20,w = 16.9 S and D_20,w = 3.19 × 10⁻⁷ cm²/s.

Fractionated apoHoSF (fraction # 1 of Fig. 9)

apoHuHF as isolated and DTT treated (curve c, Fig. 5)