This paper presents data on adsorption of immunogamma globulin (IgG) onto synthetic rodlike calcium hydroxyapatite particles (CaHaps) with various particle lengths and calcium/phosphate (Ca/P) atomic ratios ranging from 1.54 to 1.65 and compares the obtained results to those of acidic (bovine serum albumin, BSA), neutral (myoglobin, MGB), and basic (lysozyme, LSZ) proteins reported before. The effect of electrolyte concentration on IgG adsorption was also examined. The initial rate of IgG adsorption was similar to that of BSA and was slower than that of MGB and LSZ. This fact was interpreted by the difference in the structural stability and molecular weight of these proteins. The isotherms of I-G adsorption onto the CaHap particles were of pseudo-Langrnuir type. The saturated amount of adsorbed IgG IgG values (n(s)(IgG)) for the particles with mean particle length less than 70 nm decreased with increasing Ca/P ratio. The adsorption behavior of IgG molecules was very similar to that of basic LSZ, though IgG has zero net charge. The n(s)(IgG) value was increased with increased mean particle length of CaHaps; the relationship was less significant than that for BSA but similar to those for MGB and LSZ. The similar adsorption behavior of IgG and LSZ suggested that the F-ab parts of IgG molecules preferentially adsorb onto CaHap to provide the reversed Y-shaped conformation of IgG. The change of the adsorption mode of IgG molecules from the reversed Y-shaped conformation NG to side-on by "spreading" the F-c part of IgG molecules onto the particle surface over a longer adsorption time was suggested. The n(s)(IgG)value was increased with increasing electrolyte concentration by screening the intra- and intermolecular electrostatic interactions of proteins. (C) 2004 Elsevier Inc. All rights reserved.