Bovine serum albumin(BSA) was solubilized into the reverse micellar phase consisting of sodium bis(2-ethylhexyl) sulfosuccinate(AOT) and isooctane using the phase transfer method. Of particular interest in this study were the effects of pH and the added salt type and concentration on the solubilization efficiency. When univalent or divalent salts such as KCl, NaCl, $MgCl_2$, or $CaCl_2$ were added to the aqueous phase at a concentration of 0.1 M, maximum solubilization efficiency was attained at a pH ranging from 5 to 7, depending on the added salt type. Increased salt concentration up to 1 M resulted in an increased solubilization efficiency for $CaCl_2$ and NaCl, while the addition of $MgCl_2$ beyond 0.1 M showed an anomalous trend. Further, it was noteworthy that too a large extent the protein precipitated in the interface between the organic and aqueous phases at lower pHs and lower salt concentrations. The size of the reverse micelle water pool was estimated by measuring the molar ratio of the surfactant to the water, $W_0$. Irrespective of pH in the aqueous phase, the resulting value of $W_0$ was almost constant, eg., 20 for $MgCl_2$ . However, the value of $W_0$ decreased with increased salt concentration in the cases of KCl and $CaCl_2$.