Isolation and cell-free translation of messenger ribonucleic acids specifying thymus-leukemia antigens.

Messenger ribonucleic acid (mRNA) for thymus-leukemia antigens, membrane-associated glycoproteins of murine leukemia cells, was obtained from polysomes of murine leukemia cells forming thymus-leukemia antigens. Polysomes forming thymus-leukemia antigens were recovered by immunoprecipitation using alloantibodies specific for the 1,2,3 determinants of the thymus-leukemia antigen complex before they were extracted with phenol-detergent. Poly(adenylic acid)-containing RNA [poly(A)-RNA] was fractionated by oligo[deoxythymidylate] [oligo(dT)]-cellulose chromatography. The mRNA obtained had a sedimentation coefficient of approximately 17 S in agreement with the predicted size necessary for forming proteins specifying thymus-leukemia antigens. In a wheat germ system, the polypeptides formed upon addition of mRNA for thymus-leukemia antigens consisted of a major product with a molecular weight of 42,000. It was larger than the nonglycosylated heavy chain molecule of 40,000 daltons formed by the cells themselves. On the cell surface thymus-leukemia antigens exist as glycosylated molecules of 47,000 daltons associated with a light-chain equivalent to beta 2-microglobulin. Molecules of 40,000 daltons were isolated from the cells cultured in the presence of tunicamycin, an inhibitor of de novo glycosylation, and by treating thymus-leukemia heavy chains with endo-beta-N-acetylglucosaminidase H.

[1]  R. Mage,et al.  Lactoperoxidase catalyzed radioiodination of cell surface immunoglobulin: incorporated radioactivity may not reflect relative cell surface Ig density. , 1979, Journal of immunology.

[2]  W. Wickner,et al.  Translational and post-translational cleavage of M13 procoat protein: extracts of both the cytoplasmic and outer membranes of Escherichia coli contain leader peptidase activity. , 1979, Proceedings of the National Academy of Sciences of the United States of America.

[3]  P. Cossart,et al.  The primary structure of Escherichia coli K12 aspartokinase I-homoserine dehydrogenase I. Site of limited proteolytic cleavage by subtilisin. , 1978, The Journal of biological chemistry.

[4]  Y. Burstein,et al.  Primary structures of N-terminal extra peptide segments linked to the variable and constant regions of immunoglobulin light chain precursors: implications on the organization and controlled expression of immunoglobulin genes. , 1978, Biochemistry.

[5]  E. Gelfand,et al.  Human thymus-leukemia-associated antigen: isolation and partial characterization. , 1978, Journal of the National Cancer Institute.

[6]  L. Old,et al.  Immunogenetics of cell surface antigens of mouse leukemia. , 1977, Annual review of genetics.

[7]  E. Cohen,et al.  Detection of thymus leukemia antigens on the surface membranes of murine leukemia cells resistant to thymus leukemia antibodies and guinea pig complement. , 1977, Journal of the National Cancer Institute.

[8]  E. Vitetta,et al.  Molecular similarities between the Qa-2 alloantigen and other gene products of the 17th chromosome of the mouse , 1977, The Journal of experimental medicine.

[9]  J. Klein,et al.  Structural studies of H-2 and TL alloantigens. , 1977, Cold Spring Harbor symposia on quantitative biology.

[10]  E. Cohen,et al.  Estimation of the number of nucleotide sequences in mouse DNA complementary to messenger RNAs specifying a complete mouse immunoglobulin. , 1976, Biochemistry.

[11]  J. Klein,et al.  Beta 2-microglobulin is selectively associated with H-2 and TL alloantigens on murine lymphoid cells , 1976, The Journal of experimental medicine.

[12]  D. Steiner,et al.  Cell-free synthesis of rat preproinsulins: characterization and partial amino acid sequence determination. , 1976, Proceedings of the National Academy of Sciences of the United States of America.

[13]  T. Kindt,et al.  Homology in amino-terminal sequence of precursors to pancreatic secretory proteins. , 1975, Proceedings of the National Academy of Sciences of the United States of America.

[14]  B. Dobberstein,et al.  Transfer to proteins across membranes. II. Reconstitution of functional rough microsomes from heterologous components , 1975, The Journal of cell biology.

[15]  B. Dobberstein,et al.  Transfer of proteins across membranes. I. Presence of proteolytically processed and unprocessed nascent immunoglobulin light chains on membrane-bound ribosomes of murine myeloma , 1975, The Journal of cell biology.

[16]  P. A. Peterson,et al.  The subunit structure of thymus leukemia antigens. , 1975, Biochemistry.

[17]  J. Tkacz,et al.  Tunicamycin inhibition of polyisoprenyl N-acetylglucosaminyl pyrophosphate formation in calf-liver microsomes. , 1975, Biochemical and biophysical research communications.

[18]  P. A. Peterson,et al.  Thymus leukaemia antigen contains β2-microglobulin , 1975, Nature.

[19]  J. Taylor,et al.  Isolation of hen oviduct ovalbumin and rat live albumin polysomes by indirect immunoprecipitation. , 1974, The Journal of biological chemistry.

[20]  I. Schechter.  Use of antibodies for the isolation of biologically pure messenger ribonucleic acid from fully functional eukaryotic cells. , 1974, Biochemistry.

[21]  E. Cohen,et al.  Studies on the effect of specific antisera on the metabolism of cellular antigens. I. Isolation of thymus leukemia antigens. , 1974, Journal of immunology.

[22]  F. Maley,et al.  Purification and properties of an endo-beta-N-acetylglucosaminidase from Streptomyces griseus. , 1974, The Journal of biological chemistry.

[23]  B. Paterson,et al.  Efficient translation of tobacco mosaic virus RNA and rabbit globin 9S RNA in a cell-free system from commercial wheat germ. , 1973, Proceedings of the National Academy of Sciences of the United States of America.

[24]  P. Leder,et al.  Purification of biologically active globin messenger RNA by chromatography on oligothymidylic acid-cellulose. , 1972, Proceedings of the National Academy of Sciences of the United States of America.

[25]  R. Palmiter,et al.  Identification and isolation of ovalbumin-synthesizing polysomes. I. Specific binding of 125 I-anti-ovalbumin to polysomes. , 1972, The Journal of biological chemistry.

[26]  L. Old,et al.  Modulation of TL (thymus-leukemia) antigens by Fab-fragments of TL antibody. , 1968, Journal of immunology.

[27]  L. Old,et al.  Modification of the antigenic structure of the cell membrane by thymus-leukemia (TL) antibody. , 1967, Proceedings of the National Academy of Sciences of the United States of America.