The H1 histones and their interphase phosphorylated states in differentiated and undifferentiated cell lines derived from @entity19 XXXX .

@entity14641 @entity7263 @entity3208 @entity19 @entity6546 @entity189 @entity49940 @entity1391 @entity71213
The histone H1 fraction from the @entity19 @entity189 cell line F9 can be resolved by two-dimensional gel electrophoresis into at least 15 components. Ten of these components incorporate 32P from administered @entity6546 . The digestion of 3H- and @entity7263 -labeled samples with alkaline phosphatase indicates that this cell line has at least five H1 subtypes, three of which have not been observed in the @entity19 before. Every subtype is phosphorylated to some extent. There are, however, striking differences among them in the degree of phosphorylation in interphase, both in the proportion of molecules present as phosphorylated forms and in the numbers of @entity1391 groups per molecule. Phosphorylations of two types are discernible; most phosphorylations do not significantly affect the mobility of the protein in @entity3208 -containing gels but one does, probably reflecting a phosphorylation-induced alteration in protein conformation. Four subtypes undergo only the first type of phosphorylation; the other subtype undergoes both types of phosphorylation. The same 5 subtypes are also present in two other independently derived @entity189 cell lines. In contrast, two differentiated (endoderm-like) cell lines derived from @entity14641 lack @entity49940 , and one also lacks @entity71213 . Our results are consistent with the view that the H1 subtypes differ from each other functionally. They also show that neither @entity49940 nor @entity71213 is essential for cell division.
