-transparent.png){kind=logo}
Actinomycin D was found to block binding of a monoclonal antibody to nucleolar phosphoprotein 37/5.2 (B23) when incubated either simultaneously with or prior to addition of the antibody. Daunorubicin had no significant blocking activity of this antigen-antibody reaction. In comparative studies with a monoclonal antibody to nucleolar phosphoprotein 110/5.2 (C23), actinomycin D exhibited little blocking activity. When a 42-mer peptide containing the epitope of protein 37/5.2 (B23) was tested as the antigen, similar inhibition by actinomycin D of binding of the monoclonal antibody was found. These results provide evidence for binding of actinomycin D to a specific epitope of protein 37/5.2 (B23).
R K Busch, and
P K Chan, and
H Busch
November 1989,
Biochemistry,
R K Busch, and
P K Chan, and
H Busch
December 1972,
Biochimica et biophysica acta,
R K Busch, and
P K Chan, and
H Busch
October 1992,
International journal of cancer,
R K Busch, and
P K Chan, and
H Busch
March 1981,
Life sciences,
R K Busch, and
P K Chan, and
H Busch
July 1987,
Biochimica et biophysica acta,
R K Busch, and
P K Chan, and
H Busch
February 1999,
Journal of cell science,
R K Busch, and
P K Chan, and
H Busch
August 1964,
Cancer research,
R K Busch, and
P K Chan, and
H Busch
September 1989,
Arthritis and rheumatism,
R K Busch, and
P K Chan, and
H Busch
August 1989,
Biochemical and biophysical research communications,
R K Busch, and
P K Chan, and
H Busch
June 1974,
Experimental cell research,
