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Results for “Poly dA-dT”

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At least 37 records · Page 2Linked to original sources
PubMed1977

Glucocorticoid receptor-steroid complex binding to DNA. Competition between DNA and DNA-cellulose.

The binding of the glucocorticoid receptor-steroid complex from a line of rat hepatoma tissue culture (HTC) cells to DNA has been examined. An equilibrium competition assay involving a constant, low total amount of double-stranded DNA was developed to compare the complex binding ability of DNA free in solution and bound to cellulose. This binding ability is lowered by a factor of five when DNA is associated with cellulose. Similar studies with HTC cell, calf-thymus, and Escherichia coli DNA revealed no difference in the relative number or affinity of binding sites for receptor-steroid complex in each DNA. The synthetic DNA molecules poly[d(A-T)-d(A-T)] and poly[d(G-C)-d(G-C)] bound complexes equally well but less than the three "natural" DNA molecules. This appears to be due to differences in acceptor site affinity and suggests that nucleotide complexity and/or sequence influences the affinity of HTC cell receptor-glucocorticoid complexes for DNA.

Binding, Competitive↗
PubMed1978

Circular dichroism studies of the interaction of a limited hydrolysate of T4 gene 32 protein with T4 DNA and poly[d(A-T)].poly[d(A-T)].

gp32 I is a protein with a molecular weight of 27 000. It is obtained by limited hydrolysis of T4 gene 32 coded protein, which is one of the DNA melting proteins. gp32 I itself appears to be also a melting protein. It denatures poly[d(A-T)].poly[d(A-T)] and T4 DNA at temperatures far (50-60 degrees C) below their regular melting temperatures. Under similar conditions gp32 I will denature poly[d(A-T).poly[d(A-T)] at temperatures approximately 12 degrees C lower than those measured for the intact gp32 denaturation. For T4 DNA gp32 shows no melting behavior while gp32 I shows considerable denaturation (i.e., hyperchromicity) even at 1 degree C. In this paper the denaturation of poly[d(A-T)].poly[d(A-T)] and T4 DNA by gp32 I is studied by means of circular dichroism. It appears that gp32 I forms a complex with poly[d(A-T)]. The conformation of the polynucleotide in the complex is equal to that of one strand of the double-stranded polymer in 6 M LiCl. In the gp32 I DNA complex formed upon denaturation of T4 DNA, the single-stranded DNA molecule has the same conformation as one strand of the double-strand T4 DNA molecule in the C-DNA conformation.

Circular Dichroism↗
PubMed1976

Safety of viral vaccine cell substrates: a reevaluation.

Primary cultures of African green monkey kidney and rabbit kidney as well as diploid cell lines WI-38 and DBS-FRhL-2 were examined for evidence of tumorigenicity and latent RNA tumor viruses. Cells inoculated into immunosuppressed newborn hamsters and rhesus monkeys were not tumorigenic. Cells treated with 2'-deoxy-5-iodouridine to induce the production of latent viruses were examined by electron microscopy, density gradient centrifugation, and the reverse transcriptase enzyme assay. No evidence was found for RNA tumor viruses by the biochemical or biophysical methods used. The results indicated that each type of mammalian cell currently used in the production of virus vaccines would be acceptable for these parameters of safety if similar control procedures were applied at the time the vaccines were manufactured.

Animals↗
PubMed1978

Studies on the purification and properties of a 6.8-S DNA polymerase activity found in calf-thymus DNA polymerase-alpha fraction.

The heterogeneity of calf thymus DNA polymerase-alpha has been further investigated. In particular, an enzyme (enzyme D) which exhibits higher activity on poly(dA) . (dT)10 (A:T = 20:1) compared with that on activated DNA, has been further purified and its properties compared with two other activities of the DNA polymerase-alpha fraction (enzymes A1 and C) which do not show a preference for poly(dA) . (dT)10 over activated DNA. As with A1 and C, enzyme D was shown to have many of the characteristic properties of DNA polymerase-alpha in that it is an acidic protein as judged by its binding to DEAE-cellulose, has a molecular weight of about 140000, does not use a poly (A) . (dT)10 template-initiator complex and is inhibited by N-ethylmaleimide. It exhibits anomalous gel filtration behaviour on Sepharose 6B and it binds relatively weakly to DNA-cellulose compared with DNA polymerase-beta. The extreme sensitivity of enzyme D to inhibtion by N-ethylmaleimide distinguishes it from A1 and C, as does its elution position from a DEAE-cellulose column. On the other hand enzymes C and D are readily inactivated by heating at 45 degrees C unlike enzyme A1. The possible interrelationships of the multiple activities of calf thymus DNA polymerase-alpha are discussed.

Animals↗
PubMed1978

A deoxyribonucleic acid unwinding protein isolated from regenerating rat liver. Physical and functional properties.

A DNA-unwinding protein has been purified from regenerating rat liver cytosol to apparent homogeneity. The protein is present in about 10(6) copies per cell. It is a tetramer, composed of 25,000-dalton subunits which does not exhibit enzymatic activity for ATPase, DNA polymerase, or DNase. The protein is able to unwind the double helix of poly[d(A-T)], depressing the melting point of this synthetic polymer by about 40 degrees. It also binds to supercoiled SV40 DNA, probably by melting A-T-rich regions in the genome. The fully saturated complex of protein and SV40 DNA sediments at 30 S. Homologous DNA polymerases-alpha and -beta are stimulated by the protein at a different level depending on the templates used. This result argues in favor of the intervention of the unwinding protein in replication processes.

Animals↗
PubMed1977

Characterization of a new reverse transcriptase of possibly cellular origin in the chicken system.

The properties of an RNA-dependent DNA polymerase, which occurs ubiquitously in the allantoic fluid of uninfected, leukosis-virus-free eggs, are described. It is shown that the enzyme can synthesize faithful transcripts from natural RNA (globin mRNA). With biochemical and immunological methods, the enzyme can be clearly distinguished from the reverse transcriptases of the known chicken RNA tumour viruses and therefore seems to be a member of a so far unknown class of chicken polymerases. Our data show that in the chicken system reverse transcriptase can occur without connection to the replication of RNA tumour viruses and without relationship to the induction of malignancy.

Animals↗