Effects of cold, starvation and immobilization on the composition of acid-soluble nuclear proteins in chicken liver.
Nuclear proteins soluble in 0.2 M sulphuric acid were isolated from the liver of three groups of hens subjected for 60 hours to starvation, immobilization or cold exposure. The obtained proteins were separated by means of one-dimensional and two-dimensional electrophoresis on polyacrylamide gel. It was observed that this exposure of the birds to stress caused no qualitative changes in liver nuclear proteins. Histones, histone-like proteins - M1, M2, M3, uM1, HMG 1 and 2 proteins, and a large group of non-histone protein fractions gave nearly identical patterns. However, several components of nuclear proteins were found whose quantity changed in the liver of the birds subjected to stress. These changes were observed in a protein with molecular weight about 27 000 daltons and two proteins weighing over 100 000 daltons.
D000818:Animals; D002467:Cell Nucleus / Q000378:metabolism*; D002645:Chickens; D003080:Cold Temperature; D005260:Female; D008099:Liver / Q000648:ultrastructure*; D009698:Nucleoproteins / Q000378:metabolism*; D012149:Restraint, Physical; D012995:Solubility; D013217:Starvation; D013464:Sulfuric Acids / Q000494:pharmacology
D009698:Nucleoproteins; D013464:Sulfuric Acids; C033158:sulfuric acid