Bisection of a Lysine-rich Histone by N-Bromosuccinimide

Immunochemical specificity in lysine-rich histone subfractions.

Antibodies to purified calf thymus Fl, and to chromatographically purified subfractions of calf thymus Fl histones were induced by immunization of rabbits with histone-RNA complexes. Complement fixation studies with these antibodies demonstrated structural differences between the subfractions in one organ and between those of different organs and species. The anti-F1 sera showed varying reactiv...

Relationship between chromosome condensation and metaphase lysine-rich histone phosphorylation

Treatment of metaphase HTC cells with ZnCl2 inhibits histone phosphatase activity and leads to an increase in the hyperphosphorylated forms of the lysine-rich (F1) histone. Under normal conditions a massive phosphatase activity is triggered as the cells shift from M into G1 phase. In the presence of ZnCl2 this activity is abolished and thehyperphosphorylated form of F1 persists intact into G1. ...

A large scale procedure for isolation of the glycine-rich, arginine-rich histone and the arginine-rich, lysine-rich histone in a highly purified form.

1. A procedure is presented for large scale fractionation of arginine-rich histones by exclusion chromatography. With this method, 2 to 3.5 g of histone Fractions 2a and 3 were fractionated. The two fractions contained the same histone components, but they differed in the amounts of each component. 2. In histone Fraction 2a, the glycine-rich, arginine-rich (GAR) histone accounted for approximat...

Assay of protein kinase C with an N-bromosuccinimide-cleavage fragment of histone H1.

N-Bromosuccinimide cleavage of a lysine-rich histone fraction (histone III-S) yields a peptide substrate, purified by reverse-phase h.p.l.c., for the Ca2+ + phospholipid-dependent protein kinase (protein kinase C). This substrate displays no reactivity with the cyclic AMP-dependent protein kinase, and may prove useful for the detection of protein kinase C activity in crude tissue extracts.

Studies on histones. 8. A degradation product of lysine-rich histone.