Abstract
Methyl mercury chloride administered subcutaneously to hens transferred to their eggs and the major part of mercury in eggs existed as methyl mercury complex with the protein of the egg white. Egg white powder obtained by treatment with ether and acetone was dissolved in water. The protein containing methyl mercury in the solution was salted out by adding 30-60% of ammonium sulphate. The protein which was salted out was again dissolved in water by dialysis, and the protein solution was fractionated in tubes of a fraction collector through Sephadex G 100. Protein in the solution of each tube was fractionated by electrophoresis through a cellulose acetate membrane. The albumin fraction contained mercury.
The same protein solution was fractionated by Disk-electrophoresis apparatus using polyacrylamide gel (pH 9.4), and protein and mercury in each tude were quantitatively determined. Solution of the tubes in which contents of protein and mercury were high was lyophilized. The lyophilized protein powder which was dissolved in veronal buffer solution containing 0.1M natrium chloride was analyzed by an ultracentrifuger (rotor speed 60, 000rpm). The calculated sedimentation constant (S20, w) was 3.44× 10-13m/sec (dyne/g) (≈3.4S) as V was taken for 0.748.
