Abstract
Normal and starved adult chickens were injected intraperitoneally with D-galactosamine hydrochloride (0.5 g/kg body weight) and 6 h later liver chromatin acid-soluble proteins were isolated. These proteins were resolved by a two-dimensional polyacrylamide gel electrophoresis in the presence of non-ionic detergent, Triton X-100, in the first dimension and anionic detergent, sodium dodecyl sulfate, in the second dimension. Although spotting patterns of acid-soluble chromatin proteins were remarkably similar between normal and starved control birds and those receiving D-galactosamine, a disappearance of a 24-kDa protein after administration of this agent was found. Moreover, it was shown that this protein was also completely absent in the chicken erythrocyte chromatin which was known to be inactive in RNA synthesis. It seems that the disappearance of the 24-kDa chromatin protein may be associated with inhibiting of transcription in hen liver after D-galactosamine administration and during hen erythrocyte maturation.
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