Interaction of histones with human serum proteins.
The authors describe the interactions of whole calf thymus histone and its fractions with the human serum proteins. Immunoelectrophoretic analysis revealed two types of interactions: 1) a decrease in the electrophoretic mobility of a whole, immunochemically uniform fraction, and 2) a decrease in the electrophoretic mobility of only some molecules of such a fraction. In this association, the arginine-rich histone fraction (F3) was found to be the most active. The findings are important for interpreting the results of biological treatments.
D000818:Animals; D001798:Blood Proteins / Q000378:metabolism*; D002417:Cattle; D006657:Histones / Q000097:blood*; D007136:Immunoglobulins / Q000302:isolation & purification; D008075:Lipoproteins, HDL / Q000097:blood; D008077:Lipoproteins, LDL / Q000097:blood; D008259:Macroglobulins / Q000378:metabolism; D013950:Thymus Gland / Q000378:metabolism
D001798:Blood Proteins; D006657:Histones; D007136:Immunoglobulins; D008075:Lipoproteins, HDL; D008077:Lipoproteins, LDL; D008259:Macroglobulins