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glycosidase/sarkoma
Nuoroda įrašoma į mainų sritį
Puslapis 1 nuo 17 rezultatus
Glycosidases in normal and regenerating chicken liver, hepatoma Mc-29, Rous sarcoma, in turkey poult liver and hemocytoblastomes, provoked by the leukosis virus strain Mc-31.
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Four glycosidases (beta-galactosidase, alpha-mannosidase, alpha-fucosidase and beta-N-acetylglucosaminidase) were studied in chicken normal and regenerating liver, in turkey poult liver and in virus induced avian tumors--chicken hepatoma (strain Mc-29), Rous sarcoma (strain Schmidt-Ruppin) and
Surface biochemical changes accompanying primary infection with Rous sarcoma virus. II. Proteolytic and glycosidase activity and sublethal autolysis.
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Characterization of factors stimulating differentiation of mouse myeloid leukemia cells from a Yoshida sarcoma cell line cultured in serum-free medium.
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A clone, YS-T22, of cells from Yoshida sarcoma cell line, YSSF-212T, grown in "serum-free" culture medium produced factors stimulating differentiation of mouse myeloid leukemia cells (M1) to macrophages and granulocytes. The formation of macrophages and granulocytes was accompanied by induction of
Separation of the tumor rejection antigen of Rous sarcoma virus-induced murine fibrosarcoma.
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The tumor antigen capable of inducing tumor resistance (tumor rejection antigen; TRA) was separated and some of its physicochemical properties were characterized. Cytosol and plasma membrane fractions were separated from Rous sarcoma virus (RSV)-induced CSA1M tumor cells. Immunization with membrane
Transformation-dependent alterations in the oligosaccharides of Prague C Rous sarcoma virus glycoproteins.
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The influence of cell transformation on the glycosylation of viral envelope glycoproteins was examined by high-resolution gel filtration and specific glycosidase digestions of 3H-sugar-labeled glycopeptides from nondefective and transformation-defective Prague C strains of Rous sarcoma virus
Rous sarcoma virus glycoproteins contain hybrid-type oligosaccharides.
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Examination of [3H]mannose-labeled glycopeptides from Prague C Rous sarcoma virus gp85 with gel filtration and sequential glycosidase digestions demonstrated the presence of hybrid-type asparaginyl-oligosaccharides. The major hybrid species had an oligomannosyl core (Man5GlcNAc2-ASN) characteristic
Both acidic-type and neutral-type asparaginyl-oligosaccharides of host-cell glycoproteins are altered in Rous-sarcoma-virus-transformed chick-embryo fibroblasts.
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In comparisons of [3H]mannose-labelled glycopeptides from chick-embryo fibroblasts infected and transformed with non-defective Prague C Rous-sarcoma virus and from untransformed fibroblasts infected with a transformation-defective derivative of Prague C Rous-sarcoma virus, we have detected
Glycosidase analysis of large acidic-type glycopeptides from viral and cellular membrane glycoproteins. Evidence for a common oligomannosyl core with branch sugar heterogeneity.
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The asparagine-linked oligosaccharides of the complex acidic-type from [3H]mannose-, [3H]glucosamine- or [3H]galactose-labelled membrane glycoproteins of BHK21 cells and Rous-sarcoma virus were analysed by gel filtration combined with extensive digestion with endo- and exo-glycosidases from
Rous sarcoma virus-transformed baby hamster kidney cells express higher levels of asparagine-linked tri- and tetraantennary glycopeptides containing [GlcNAc-beta (1,6)Man-alpha (1,6)Man] and poly-N-acetyllactosamine sequences than baby hamster kidney cells.
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The alterations in complex-type N-linked oligosaccharides that can occur when an animal cell line is transformed by two dissimilar viruses were examined by comparing the N-linked oligosaccharides of baby hamster kidney (BHK) cells, metabolically radiolabeled with [2-3H]mannose, to the same class of
The immunogenic glycoprotein gp35-37 of human herpesvirus 8 is encoded by open reading frame K8.1.
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Human herpesvirus 8 (HHV-8) is likely to be involved in the pathogenesis of Kaposi's sarcoma (KS) and body cavity-based lymphomas (BCBLs). The HHV-8 genome is primarily in a latent state in BCBL-derived cell lines like BCBL-1, but lytic replication can be induced by phorbol esters (R. Renne, W.
Elevation of lysosomal enzymes in primary Lewis lung tumor correlated with the initiation of metastasis.
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Lysosomal enzymes were elevated about two-fold in primary s.c. Lewis lung carcinoma as compared with metastatic nodules in the lung. In a time course experiment, a general two-fold elevation of acid phosphatase and several glycosidases was observed in the primary tumor between the 14th and 17th
Detection and biochemical characterization of antigens in human leukemic sera that cross-react with primate C-type viral proteins (Mr 30,000).
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Antigens have been detected in 35 to 40% of sera from patients with leukemia that cross-react with the Mr 30,000 core proteins (p30) of baboon endogenous virus (BaEV) and/or of simian sarcoma-simian sarcoma-associated virus (SiSV) in a solid-phase enzyme immunoassay using anti-SiSV p30 and anti-BaEV
The galactoside-specific lectin from mistletoe as biological response modifier.
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Experience with herbal extracts can guide the isolation of substances that effectively amend aspects of the host's defence system against tumor growth and spread. This capacity appears to be conferred to mistletoe (Viscum album) extract by a rather small dose range of the galactoside-specific lectin
Current advances in the diagnosis and treatment of AIDS: an introduction.
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Significant progress has been made in the diagnosis and treatment of AIDS. Laboratory tests available for assessment of human immunodeficiency virus (HIV) infection include the detection of antibodies to HIV type 1, the direct detection of the virus, the identification of surrogate markers, and the
Primer tRNA(Trp) of RSV-transformed or RAV-1-infected cells up-regulates the antiribosomal activity of gelonin.
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Some ribosome-inactivating proteins (RIPs) with RNA-N-glycosidase activity on 28S rRNA require, for maximal inactivation of ribosomes, the presence of tRNA. tRNA(Trp) specifically up-regulates gelonin, the RIP from Gelonium multiflorum. The same tRNA is the primer of the reverse transcriptase of
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