Isolation and Partial Characterization of a Nuclear Antigen (68/6.3) from the Namalwa Cell Line (a Burkitt Lymphoma)
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A nuclear antigen was purified from the 0.01 M Tris-HCl/pH8 extract of nuclei of the Burkitt tumor Namalwa cell line to electrophoretic homogeneity by DEAE cellulose chromatography, affinity chromatography, and preparative isoelectric focusing. The yield of antigens was 0.02% of the nuclear 0.01 M Tris-HCl/pH8 extract. On two-dimensional gel electrophoresis, the major antigen separated into two adjacent protein spots with molecular weights of 68,000 and an approximate pI of 6.3 (68/6.3 A and 68/6.3 B). A minor antigen had a molecular weight of 61,000 and pI of 6.0 (61/6.0). Fourteen 125I-labeled peptides were obtained from the tryptic digest of the major antigen (68/6.3 A and 68/6.3 B). The amino-acid composition analysis of the purified antigens indicated that the amino acids in the highest content were glycine (15%), glutamic acid (11.6%), and serine (9%); the ratio of acidic to basic amino acids was 1.95. In studies on nucleolytic activity, the purified antigen produced a single-stranded and then a double-stranded cleavage of PM 2 and pBR 322 DNA. This antigen is the first purified nuclear antigen that reacts with the HeLa-specific nucleolar antibodies.
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Takahashi K, Chan P, BUSCH R, Busch H J Cancer Res Clin Oncol. 1983; 105(1):67-75.
PMID: 6833342 DOI: 10.1007/BF00391834.
Busch H Mol Cell Biochem. 1984; 61(2):111-30.
PMID: 6374426 DOI: 10.1007/BF00222490.
Onc genes and other new targets for cancer chemotherapy.
Busch H J Cancer Res Clin Oncol. 1984; 107(1):1-14.
PMID: 6199358 DOI: 10.1007/BF00395484.
Immunohistochemical and biochemical characterization of antisera raised to human tumor nucleoli.
Greenfield R, Lamon M, Olech L, Grattan J J Cancer Res Clin Oncol. 1989; 115(4):351-60.
PMID: 2503520 DOI: 10.1007/BF00400962.