Open AccessImmunogenicity and Antigenic Specificity of a Glutaraldehyde Cross‐Linked Transfer RNA‐Protein Conjugate
Author(s) -
Aharonov Aharon,
Fuchs Sara,
Sela Michael,
Stollar B. David
Publication year - 1974
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1974.tb03316.x
Subject(s) - transfer rna , escherichia coli , microbiology and biotechnology , rna , immunogenicity , antigen , ribosome , bovine serum albumin , antibody , biochemistry , glutaraldehyde , ribosomal rna , biology , chemistry , chromatography , gene , genetics , immunology
tRNA‐protein conjugates were prepared by cross‐linking of tRNA to protein by means of glutaraldehyde. Antibodies were elicited in rabbits and goats immunized in complete Freund's adjuvant with the electrostatic complexes of tRNA‐protein with methylated bovine albumin. Specific antibodies were purified from the sera on a tRNA‐Sepharose immunoadsorbent. The anti‐tRNA sera bound directly 14 C‐labelled Escherichia coli tRNA. Antigen binding assay was applied for testing the specificity of the antibodies. The binding of 14 C‐labelled E. coli tRNA was inhibited by the homologous unlabelled E. coli tRNA, by yeast tRNA, by ribosomal RNA, and to a significantly lesser extent by DNA, poly(A) · poly(U) and poly(I) · poly(C). Digestion of tRNA by pancreatic RNAase abolished its binding to the antibodies.