A Disappearance of a 24-kDa Acid-Soluble Protein from Liver Chromatin of Normal and Starved Hens Following D-Galactosamine Administration Jan Palyga Department of Genetics, Educational University of Kielce, Rewolucji Pazdziernikowej 33; 25-518 Kielce. Poland Z. Naturforsch. 40c, 798—805 (1985); received August 13, 1985 D-Galactosamine, Starvation, Chicken Liver, Chromatin, Histones Normal and starved adult chickens were injected intraperitoneally with D-galactosamine hydro chloride (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. Introduction Starvation is a known factor influencing the phys iological properties of tissues by producing a hypo- metabolic environment for biochemical reactions. It has been shown [ 1] that morphology of liver nuclei was altered in rats subjected to a short period of food deprivation. Under this circumstances the condensed chromatin occupied much larger areas than in nor mal animals and the perichromatin fibrils which sur rounded it were largely absent. It has been also found [2] that fluorescent spectra of chromatin and its components —histones and nonhistone proteins — isolated from starved rats were altered in comparison with those of normal ones. Moreover, a marked dif ferences in the amount of some specific nuclear globulins with molecular weights of about 80 and 125 kDa from liver of starved rats were also ob served [3, 4], Histones play a significant role in chromatin by participating in the maintenance of chromatin struc ture and acting as repressors of template activity [5], Although histones have been well characterized many years ago [6], a detailed investigations employ ing high resolution electrophoretic methods have re vealed the existence of minor histone variants in acid Reprint requests to J. Palyga. Verlag der Zeitschrift für Naturforschung, D-7400 Tübingen 0341 - 0382/85/1100 - 0798 $01.30/0 extracts of chromatin [7—9], It has been demon strated [ 10, 11] that histone variants are additionally multiplied by attaching of ubiquitin — a nonhistone chromatin protein extractable with a low ionic strength solutions [ 12] — to the core histones, espe cially H2A and H2B, producing a series of minor histone-related proteins differing in their elec trophoretic properties. In contrast to the whole his tone bands, they have been shown to change in vari ous tissues [13, 14], mutant cells [15], during de velopment and differentiation [16—18] and following exposure to pharmacological agents [19]. Dilute solutions of hydrochloric, sulfuric or per chloric acids widely used for solubilizing of histones can also extract a certain number of other basic and/ or neutral protein components existing in minute quantities [9, 20, 21], Though they were found to be abundant in acid extracts of whole nuclei, their number and quantity decreased markedly in acid ex tracts of chromatin [7] suggesting that they were largely the nonhistone nuclear proteins readily re movable from nuclei by low ionic strength salt solu tions in the course of chromatin isolation. Some of them have been partially characterized. For exam ple, proteins C23 and B23 have been isolated from nucleoli of Novikoff hepatoma cells [22] and demon strated to be a major silver staining proteins of the nucleolar organizer [23], A high-molecular-weight acid-soluble nuclear protein similar to protein C23 has been also prepared from mouse ascities sarcoma