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Biomedical subjects

H Busch

Publications and source records attributed to H Busch.

At least 289 records · Page 16Linked to original sources

Two-dimensional polyacrylamide gel analysis on nuclear proteins from human tumor cell lines.

Two-dimensional polyacrylamide gel electrophoretic analysis was carried out on HeLa, KB, ALL and GW-39 cell "Chromatin Fraction II" proteins. Of the many proteins found, most were visualized in earlier studies on rodent tumors and normal tissues. Of these the greater density of protein CP and the presence of protein CG' differentiates tumors from the nontumor tissues. In samples of normal and mitogen stimulated human lymphocytes, protein CG' was absent and protein CP was present in small amounts. Two-dimensional patterns of 0.4N H2SO4 soluble nuclear proteins showed elevated amounts of proteins C16-18 in the GS-39 cell patterns. Proteins Hu1, G1, G2, G3 and G5 were detected only in human cell nuclei. The increased density of staining for protein CP and the presence of CG' are potential biological markers for neoplastic cells.

Animals↗

Presence of elongation factor 1 in nuclei and nucleoli of rat liver.

Purified rat liver nuclei contain 11% of the total cellular translation elongation factor 1 activity. Ninety percent of the nuclear EF-1 activity was in the nucleoplasm and 10% was nucleolar. The specific activities of the nuclear and nucleolar EF-1 were 2 to 3 times higher, respectively, than EF-1 activity of the liver homogenate. The presence of EF-1 in the purified nuclei did not result from cytoplasmic contamination since only 0.14% of the cellular lactate dehydrogenase was present in the nuclei. These results provide the first evidence for the presence in the cell nucleus of translational factors of protein synthesis.

Animals↗

Purification and partial characterization of protein 35/7.7 a cytosol protein that is abundant in rapidly growing hepatomas.

Protein 35/7.7 is an abundant cytosol protein of Morris hepatoma 3924A and Novikoff hepatoma which was not found in normal liver. Protein 35/7.7 was isolated from the cytosol of Novikoff hepatoma ascites cells by ammonium sulfate precipitation and DEAE-cellulose chromatography. It migrated as a single major spot on two-dimensional isoelectric focusing-SDS polyacrylamide gels. The N-terminal hexapeptide is Val-Asx-Pro-Thr-Val-Phe and its carboxyl-terminal amino acid is phenylalanine.

Amino Acid Sequence↗

Enrichment of special Novikoff hepatoma and regenerating liver mRNA by hybridization to cDNA-cellulose.

Total polysomal poly(A)+ RNA of Novikoff hepatoma and of 18-hr regenerating rat liver were compared by analysis of their in vitro translational products on two-dimensional isofocusing/sodium dodecyl sulfate gels. This technique resolved the translated proteins sufficiently to permit detection of quantitative and some qualitative differences between the two mRNA populations. Excess cDNA from regenerating liver or Novikoff hepatoma, covalently linked to cellulose, was used to adsorb the complementary mRNA sequences from Novikoff hepatoma or regenerating liver. As shown by two-dimensional gel electrophoresis, the translated products of the bound mRNA fractions contained proteins common to both tissues. Novikoff hepatoma mRNA which did not bind to regenerating liver cDNA was enriched in sequences encoding for proteins 11/5.1, 15/6.8, 40/8.2, and 65/5.1 (shown as molecular weight/pI). These polypeptides were not detectable in the translational products of regenerating liver mRNA. Regenerating liver mRNA that was not bound to Novikoff hepatoma cDNA was enriched in sequences coding for proteins 12.5/4.9, 13.5/7.4, 17/8.2, 24/5.5, and 46/6.4; these proteins were not found in the translational pattern from Novikoff hepatoma. These results show that adsorption of mRNA to solid-phase cDNA provides a valuable technique for differentiating mRNA species in related tissues and for corresponding enrichment of these specific mRNAs.

Animals↗

Characterization of N6, O2-dimethyladenosine from nuclear RNA of Novikoff hepatoma.

A modified nucleoside was isolated from low molecular weight nuclear RNA of Novikoff hepatoma, the nucleotide sequence of which was reported earlier. The structure of this novel nucleoside was shown to be N6, O2'-dimethyladenosine (m6Am) by mass spectrometry of its trimethylsilyl derivative and by comparison with the mass spectra of N6- and O-2' monmethyl model compounds. The complete characterization was carried out using 0.04 A260 units (2 microgram) of m6Am.

Adenosine↗

Comparative ultrastructural studies of nucleoli of tumor cells treated with adriamycin and the newer anthracyclines, carminomycin and marcellomycin.

This study was designed to determine the effects of several antitimor anthracyclines, including Adriamycin and its analogs, carminomycin and marcellomycin, on the ultrastructure of nucleoli of Novikoff hepatoma cells. Adriamycin and carminomycin, which are structurally related, induce nucleolar segregation following the formation of conspicuous fibrillar centers. Marcellomycin did not induce formation of nucleolar fibrillar centers. Instead, numerous microspherules formed following treatment with marcellomycin; later complete nucleolar segregation developed. The microspherules were observed to be in various stages of extrusion from the nucleolar body. This microspherule "migration" appeared to be both time and drug concentration dependent. These results show that the rate and extent of nucleolar ultrastructural aberration may be related to structural differences of the various anthracyclines.

Animals↗

Chromatin-associated glycoproteins of normal rat liver and Novikoff hepatoma ascites cells.

Glycoproteins were demonstrated in the 0.6 M NaCl extract of chromatin of normal liver and Novikoff hepatoma cells by periodic acid-Schiff staining of sodium dodecyl sulfate-polyacrylamide gels. In chromatin extracts of Novikoff hepatoma cells, six major periodic acid-Schiff-positive bands coincident with Coomassie Blue-stained protein bands were found with molecular weights of 30,000, 54,000, 64,000, 75,000, 104,000, and 127,000. A corresponding extract from normal rat liver chromatin revealed the presence of four major periodic acid-Schiff-positive bands that migrated with protein bands at molecular weights of 16,000, 30,000, 54,000, and 75,000. The glycoproteins of these extracts contained either mannose or alpha-D-glucose, fucose, and N-acetylglucosamine as shown by the specificity of lectins in affinoelectrophoresis. One of the glycoproteins detected by affinoelectrophoresis was very basic.

Animals↗

Isolation and characterization of a cytosol protein (64/7.2) present in large amounts in rapidly growing hepatomas.

Protein 64/7.2 (molecular weight/isoelectric point) is present in the cytosol of several hepatomas including the Novikoff hepatoma and Morris hepatomas 9618A, 7794A, and 3924A, but it is not present in liver or 18-hr regenerating liver. Quantitatively, its concentration was highest in Novikoff hepatoma (150 microgram/g tissue) and Morris hepatoma 3924A (550 microgram/g tissue), which are rapid-growing tumors, less in Morris hepatoma 7794A (72 microgram/g tissue), which is of intermediate growth rate, and least in the slow-growing Morris hepatoma 9618A (25 microgram/g tissue). Protein 64/7.2 was isolated from Novikoff hepatoma ascites cells in high purity as shown by its migration as a single band on one-dimensional acid-urea-polyacrylamide gels and a single spot on two-dimensional isoelectric focusing sodium dodecyl sulfate-polyacrylamide gels. Its amino acid composition has an acidic to basic amino acid ratio of 1.6. Its amino-terminal amino acid is lysine, and its carboxyl-terminal amino acid is glycine. Interestingly, the amino acid composition is strikingly similar to that of the phosphorylated Novikoff hepatoma chromatin Protein Cg', partially characterized in our laboratory.

Amino Acids↗

[The use of TV-technique for a quantitative evaluation of the longitudinal psychopathological profile (author's transl)].

19 depressed patients were treated with viloxazine (n = 9) or amitriptyline (n = 10) in a double-blind trial. TV-tapes produced for each patient on day 0, 10 and 20 were analyzed with respect to the global intensity of depression and to 4 other verbal or averbal psychopathological parameters by 4 independent raters under the condition of a time-blind analysis. Global intensity of depression, prosodic, depressive contents of experience, and psychomotoric inhibition were found decreased between day 0 and day 10 for the viloxazine group, and between day 10 and day 20 for the amitriptyline-group. The accuracy of judgement of agitation was the lowest one.

Amitriptyline↗

[Synopsis of psychopathological, electroencephalographical, and pharmacokinetic variables during antidepressive treatment with viloxazine (author's transl)].

In order to achieve a more differentiated assessment of the profile and time course of treatment with a new antidepressant drug, several psychiatric, neurophysiological, and biochemical parameters were examined in a double-blind study (viloxazine versus amitriptyline). Special attention was directed to the use of a time-blind audiovisual technique. The TV technique allowed to demonstrate an earlier onset of the therapeutic effect under viloxazine, which is in good agreement with the cross-sectional and longitudinal profile of viloxazine as regards pharmacokinetics and EEG.

Amitriptyline↗

[Limitations of mass transfusion].

As a result of blood conservation there is nearly no limit to transfusion therapy. This is shown by reviews of the University Clinic of Hamburg-Eppendorf. A still existent limitation in patients with irregular antibodies requires a supraregional cooperation the possibilities of which are discussed. In intensive care medicine an especially critical indication is necessary. Blood transfusion in hopeless cases (ut aliquid fiere) is as unjustifiable as artificial respiration is in patients having an EEG 0-line.

Antibodies↗

Comparison of adriamycin-induced nucleolar segregation in skeletal muscle, cardiac muscle, and liver cells.

Male Sprague-Dawley rats were treated with either 2.5, 3.5, or 5.0 mg/kg of adriamycin by iv injection. After 1 or 3 hours of treatment, samples of liver, cardiac muscle, and skeletal muscle cells were examined by electron microscopy. The changes in ultrastructure observed in these tissues after the first hour included nucleolar segregation and altered distribution of the perinucleolar chromatin. However, no alterations in the ultrastructure of either the nucleus or cytoplasm were observed in tissues examined 3 hours after a 5-mg/kg dose of adriamycin. The doses at which nucleolar alterations occurred varied between tissues. In skeletal and cardiac muscle cells, marked alterations in nucleolar ultrastructure were observed at doses of 3.5 and 5.0 mg/kg of adriamycin. Liver cell nucleoli, however, exhibited few structural aberrations at these doses. The similarities in response of skeletal and cardiac muscle suggest that ultrastructural analysis of skeletal muscle biopsies may be useful in evaluating adriamycin cardiotoxicity.

Animals↗