Summary
Rabbit antisera obtained by immunization with poly-L-lysine-phosphorylated bovine serum albumin reacted with free whole histone, free F1(A) and free Fw as well as with whole histone and all the histone fractions coupled to human serum albumin with the carbodiimide reagent. Free whole histone and the histone fractions inhibited the reaction of these poly-L-lysine antisera with poly-L-lysine and the order of inhibitory effectiveness paralleled the lysine content of whole histone and the histone fractions. Antibodies obtained by immunization with the carbodiimide coupled poly-L-lysine reacted with poly-L-lysine, whole histone and the histone fractions coupled to human serum albumin but did not react with free poly-L-lysine, free whole histone or the free histone fractions. The sera obtained after immunization with poly-L-lysine coupled to human serum albumin contained only 7 S antibodies whereas those obtained following immunization with poly-L-lysine-phosphorylated bovine serum albumin contained both 7 S and 19 S antibodies. The 7 S fraction reacted more efficiently with poly-L-lysine and the 19 S with free F1(A). Whole histone and the histone fractions did not react with a poly-D-lysine antiserum nor did they inhibit the reaction between poly-D-lysine and a poly-D-lysine antiserum. Whole histone and the histone fractions, whether free or coupled, did not react in C′ fixation with a nonimmune rabbit serum or a nonrelated rabbit serum such as anti-ribonuclease. Direct reactivity was observed between the poly-L-lysine-phosphorylated bovine serum albumin antisera and another basic protein, ribonuclease, and with deoxyribonucleoprotein but less than 20% C′ fixation occurred with cytochrome c, lysozyme, human serum albumin or pepsin.
Footnotes
This work was performed under Grant GB-5606 from the National Science Foundation.
