[Immunohistochemical studies of the gastric somatostatin-containing D-cells in the diabetic rat following pancreatic transplantation].
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Biomedical subjects
Publications and source records attributed to H Fujitani.
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Nuclear antigen in Novikoff hepatoma chromatin was partially purified and characterized. As indicated by complement fixation assay, this antigen was present in chromatin of embryonic livers and several transplantable tumors. It was not detected in normal tissue chromatins of the same animals. For its immunological specificity this protein antigen (molecular weight 45,000-60,000) had to be complexed with DNA. Preliminary experiments indicate that specific nuclear protein antigens are also present in human tissues and spontaneous malignancies.
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A group of chromosomal non-histone proteins with affinity for DNA (NP) was isolated from rat liver and Novikoff hepatoma. This fraction, which represents less than 5% of the total chromatin protein content, binds preferentially to unique, double-stranded sequences of fractionated homologous DNA. The interactions are strong at low ionic strength (Km = 6.7 X 10(-9) M) and decrease with rising salt concentration. Complexes of the NP protein fraction with homologous DNA are immunologically tissue-specific. As determined by microcomplement fixation, the NP proteins in Novikoff hepatoma are associated with the transcriptionally active, diffuse fraction of chromatin.
A fractionation schedule is described which allows the isolation of a group of chromosomal non-histone proteins (NP) with affinity for DNA. In polyacrylamide gel electrophoresis these proteins isolated from rat liver are represented principally by a group of low molecular weight polypeptides. The NP fraction comprises about 2-4% of the total chromatin protein content in rat liver or Novikoff hepatoma. Experiments in vivo and in vitro revealed that the NP proteins do not incorporate significant amounts of 32P. Complexes of the chromosomal proteins NP with homologous DNA are immunologically tissue specific and the specificity can be transferred by reconstituting the NP proteins from one tissue to the residual chromatin from another.
Nuclear proteins of rat liver and rat ascites hepatoma were fractionated by extraction in solutions of different salt concentration and analyzed by sodium dodecyl sulfate polyacrylamide gel electrophoresis. The difference between the electrophorograms of the different fractions of nuclear proteins isolated from liver and from hepatoma was found in the bands which have the same electrophoretic mobility as the main proteins of informofers and are extracted from nuclei at salt concentrations which extract informofers. These changes in the electrophoretic patterns of proteins with the solubility and mobility of the proteins of informofers could be related to the defective processing of heterogeneous nuclear RNA in the hepatoma. In addition the identity of electrophorograms of nuclear proteins isolated from liver and from hepatoma and the identity of most bands in the electrophorograms of nuclear proteins which are soluble in 0.35 M NaCl and chromosomal proteins which are not soluble at this salt concentration support the notion that these nonhistone nuclear proteins which can be identified as the major bands in electrophorograms of chromosomal proteins are not the specific regulators of gene expression.
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