Antibodies against the folding domain of histone H5 cross-react with H1(0) but not with H1.
Antibodies to the folding domain (residues 22-100) of histone H5 were elicited in rabbits. Analysis of the specificity of these antibodies by enzyme-linked immunoassay and by diazobenzyloxymethyl cellulose transfer techniques revealed that the antibody cross-reacts strongly with intact H5 and histones H1(0)a and H1(0)b purified from ox liver but not with the four core calf thymus, or with high mobility group proteins. We conclude that the globular region of H5 is serologically homologous to that of H1 degrees and suggest that possible functional similarities between the two proteins reside in this region.
D000818:Animals; D000906:Antibodies; D000936:Antigen-Antibody Complex; D002417:Cattle; D002645:Chickens; D003429:Cross Reactions; D004797:Enzyme-Linked Immunosorbent Assay; D000939:Epitopes / Q000032:analysis; D004912:Erythrocytes / Q000737:chemistry; D006657:Histones / Q000097:blood / Q000276:immunology; D007700:Kinetics; D011487:Protein Conformation; D013950:Thymus Gland / Q000737:chemistry
D000906:Antibodies; D000936:Antigen-Antibody Complex; D000939:Epitopes; D006657:Histones