TY - JOUR
T1 - Solid phase radioimmunoassay for chromosomal components
AU - Romani, M.
AU - Vidali, G.
AU - Tahourdin, C. S M
AU - Bustin, M.
PY - 1980
Y1 - 1980
N2 - This manuscript describes the use of a solid phase radioimmunoassay for serological analysis of chromosomal components. The applicability of this assay for various studies on nonhistone chromosomal proteins, histones, and chromatin subunits is illustrated. By this technique it is possible to detect and quantify nuclear antigens in the nanogram range. The assay has all the inherent sensitivity and precision of radioimmunoassays and, as such, introduces a new, convenient method for serological analyses of chromosomal components. The results presented reconfirm the serological similarity among the HMG (high mobility group) proteins derived from various sources. The amount of HMG proteins present in mononucleosome purified from calf thymus is similar to that present in mononucleosomes purified from HeLa cells, suggesting that various tissues contain similar amounts of these proteins. Per nucleosome, dinucleosomes and trinucleosomes contain as much HMG-1 protein as mononucleosomes, suggesting that the protein is not exclusively associated with those regions of DNA which have been solubilized by micrococcal nuclease. Part of the antigenic determinants present in HMG-1 forming a complex in the nucleosomal conformation do not interact with antibodies.
AB - This manuscript describes the use of a solid phase radioimmunoassay for serological analysis of chromosomal components. The applicability of this assay for various studies on nonhistone chromosomal proteins, histones, and chromatin subunits is illustrated. By this technique it is possible to detect and quantify nuclear antigens in the nanogram range. The assay has all the inherent sensitivity and precision of radioimmunoassays and, as such, introduces a new, convenient method for serological analyses of chromosomal components. The results presented reconfirm the serological similarity among the HMG (high mobility group) proteins derived from various sources. The amount of HMG proteins present in mononucleosome purified from calf thymus is similar to that present in mononucleosomes purified from HeLa cells, suggesting that various tissues contain similar amounts of these proteins. Per nucleosome, dinucleosomes and trinucleosomes contain as much HMG-1 protein as mononucleosomes, suggesting that the protein is not exclusively associated with those regions of DNA which have been solubilized by micrococcal nuclease. Part of the antigenic determinants present in HMG-1 forming a complex in the nucleosomal conformation do not interact with antibodies.
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M3 - Article
C2 - 6153178
AN - SCOPUS:0018824072
VL - 255
SP - 468
EP - 474
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 2
ER -