Fractionation of nonhistone proeins on a column of daunomycin-CH-Sepharose 4B.
Daunomycin was coupled via its amino group to omega-carboxypentyl agarose (CH-Sepharose 4B). Nonhistone proteins from rat leukemia cells (DBLA-6) were fractionated on a column of the adsorbent. The adsorption of nonhistone proteins to the column was increased by high salt concentration (4 M NaCl) and was reversed by 20% glycerol (v/v), indicating a hydrophobic interaction. Complexity of the chromatographic patterns may reflect the occurrence of several species of binding protein in the tumor cells used. Thus the hydrophobic chromatography in the presence of a high concentration of salt was a useful method for fractionation of nonhistone proteins under non-rigorous conditions.
D000818:Animals; D002846:Chromatography, Affinity; D002868:Chromosomal Proteins, Non-Histone / Q000302:isolation & purification*; D003630:Daunorubicin; D007942:Leukemia, Experimental / Q000032:analysis; D008970:Molecular Weight; D051381:Rats; D012685:Sepharose
D002868:Chromosomal Proteins, Non-Histone; D012685:Sepharose; D003630:Daunorubicin