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Ca2+-binding proteins in nuclei.

A Schibeci·A Martonosi
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Abstract

Nuclei isolated from skeletal muscle of 15-day-old chick embryos, adult chickens, rabbits and from rat liver contain on the average 8-18 nmol Ca2+/mg protein. Digestion of nuclei with DNAase I and RNAase at 37 degrees C for 8--12 h reduced the Ca2+ binding by more than 90%. After nuclease treatment, Ca2+-binding proteins were identified in the nonhistone chromosomal protein fractions and in the insoluble residue by equilibrium dialysis and centrifuge transport, in media of 0.1 M KCl and 1 mM MgCl2. The interaction of Ca2+-binding proteins with chromatin may be of importance in the regulation of the gene expression in response to changes in cytoplasmic and nucleoplasmic free-Ca2+ concentration.

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AnimalsBinding SitesCalciumCalcium-Binding ProteinsChick EmbryoChickensChromosomal Proteins, Non-HistoneDeoxyribonuclease IDeoxyribonucleasesElectrophoresis, Polyacrylamide GelEndonucleasesLiverMusclesRabbitsRatsRibonucleasesSubcellular FractionsJournal ArticleResearch Support, Non-U.S. Gov'tResearch Support, U.S. Gov't, Non-P.H.S.Research Support, U.S. Gov't, P.H.S.

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A Schibeci, A Martonosi. 1980. Ca2+-binding proteins in nuclei.. https://doi.org/10.1111/j.1432-1033.1980.tb06132.x

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