Comparison of salt-extractable nuclear proteins of regenerating liver, fetal liver, and Morris hepatomas 9618A and 3924A.
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Biomedical subjects
Publications and source records attributed to H Busch.
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The influence of the extraction of hnRNP (informofer) particles on the ultrastructural appearance of the perichromatin granules was studied. The extraction of hnRNP particles was carried out by SAMARINA's procedure from the rat liver nuclear fraction. The extraction did not change the numbers and the general ultrastructural features of perichromatin granules. It is therefore unlikely that the perichromatin granules are the morphological representatives of storaged or transported hnRNA.
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A nucleolar chromatin antigen (NoAg-1) found in Novikoff hepatoma but not in normal liver has been purified to homogeneity as shown by two-dimensional gel electrophoresis. Initial purification of NoAg-1 was partially achieved by isolation of nucleolar chromatin and fractionation of its proteins by successive extraction with solutions of increasing salt concentration. Further purification of this antigen was achieved by affinity and hydroxylapatite chromatography. Although approximately 50% of the NoAg-1 antigen was in the 0.6 M NaCl extract of Novikoff nucleoli, it was less pure than in the 2 M NaCl:5 M urea extract which contained 25% of the NoAg-1 at a purity of 40%. The highly purified NoAg-1 had an approximate molecular weight of 60,000 and pl of 5.1; the yield of NoAg-1 was 0.22% of the total nucleolar proteins.
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With the aid of a simple silver-staining procedure, large numbers and unusual arrays of nucleolar argyrophilic granules were found in Novikoff hepatoma, KB, and HeLa cells. Some of these arrays consisted of linearly arranged discrete granules, and others were in two to three rows each containing three to five granules. Corresponding formations were not found in either the normal or regenerating liver nucleoli which contained an argyrophilic network in which the dark granules were apparently associated with the less dark argyrophilic fibrils of a reticulum. The nucleolar argyrophilic granules were readily identifiable in the separated daughter nuclei of the tumor cells in telophase, suggesting that the increased nucleolar activity of the G1 phase begins in these cells even before cell division has been completed.
Progress is expected in psychopathological diagnosis by using audiovisual procedures. Nowadays, a valid psychopathology concept should be broadly planned and the important method of description as well as understanding procedures should be considered. For such a model of psychopathology it seems appropriate to investigate the different psychopathological phenomenons as expression of a disturbed communication ability. Concerning this outlook, new strategies are to be developed or procedures of other disciplines are to be adapted for the psychopathological research. It seems attractive to anticipate aid from structuralistic and information-theoretical issues for the breaking of yet substancially less good apperceived facts. The interest hereby concentrates upon the relationship between verbal and averbal phenomenons and upon better criteria for an interpretation of the phenomenons as an expression of the subjective experience of the psychiatric patient as well as of his/her communicative competence. In order to use audio-visual techniques successfully, an orientation in specfic, originary particularities of the different methodological assessments is required. The way and extent of such problems can be demonstrated for the study of psychopathological phenomenons by the importance of the camera guide, the selection, the enlargement of a sequence, and the combination of different parts of an interview. The criteria of a field-specific TV-methodology must first be elaborated for the majority of the questioning. The user of audiovisual methods not only has to consider the special needs of the psychic ill, but also has to face critically the seduction ways of this potential medium.
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The primary structure of 18S rRNA of the Novikoff hepatoma cells was investigated. Regardless of whether the primary sequence of 18S rRNA is finally determined by RNA sequencing methods or DNA sequencing methods, it is important to identify numbers and types of the modified nucleotides and accordingly the present study was designed to localize the modified regions in T1 RNase derived oligonucleotide. Modified nucleotides found in 66 different oligonucleotide sequences included 2 m62A, 1 m6A, 1 m7G, 1m1cap3psi, 7 Cm, 13 Am, 9 Gm, 11 Um, and 38 psi residues. A number of these modified nucleotides are now placed in defined sequences of T1 RNase oligonucleotides which are now being searched for in larger fragments derived from partial T1 RNase digests of 18S rRNA. Improved homochromatography fingerprinting (Choi et al. (1976) Cancer Res. 36, 4301) of T1 RNase derived oligonucleotides provided a distinctive pattern for 18S rRNA of Novikoff hepatoma ascites cells. The 116 spots obtained by homochromatography contain 176 oligonucleotide sequences.
A nuclear nonhistone protein which decreases in chromatin during growth (Yeoman, L. C., et al. (1975) Cancer Res. 35, 1249) has been isolated in high purity from the chromatin of normal rat liver nuclei by gel electrophoresis and column chromatography. This protein, designated BA (Yeoman, L.C., et al. (1973) Biochem Biophys. Res. Commun. 53, 1067), has a molecular weight of 31 000, an acidic to basic amino acid composition ratio of 0.9, and contains one tryptophan residue per molecule. Hydrazinolysis indicated protein BA has a lysine carboxyl terminus; however, the amino terminal is blocked as no reaction occurred with dansyl chloride. Maps of tryptic peptides of protein BA contained 46 spots. Protein BA binding to various DNAs was examined by the nitrocellulose filter assay. Binding was slightly enhanced by 2mM Mn2+ion; Mg2+, however, decreased binding. Binding was optimal at neutral pH and an ionic strength of 0.2 M [NaCl]. Equilibrium competition binding studies indicated a binding preference of protein BA for dA-dT rich DNA.