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proteinase/sarkooma
Linkki tallennetaan leikepöydälle
Sivu 1 alkaen 75 tuloksia
Cysteine proteinase inhibitor in the ascitic fluid of sarcoma 180 tumor-bearing mice is a low molecular weight kininogen. Partial NH2- and COOH-terminal sequences and susceptibility to various glandular kallikreins.
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It has been proposed that a cysteine proteinase inhibitor (CPI) found in the ascitic fluid of Sarcoma 180 tumor-bearing mice is a kind of kininogen (Itoh, N., Yokota, S., Takagishi, U., Hatta, A., and Okamaoto, H. (1987) Cancer Res. 47, 5560-5565). The first 40 NH2-terminal residues and 54 residues
Thiol proteinase inhibitor in the ascitic fluid of sarcoma 180 tumor-bearing mice.
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A thiol proteinase inhibitor (TPI) has been purified from the ascitic fluid of Sarcoma 180 tumor-bearing mice. The molecular weight of the inhibitor was estimated to be 67,000 on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and the substance inhibited papain, cathepsins B and L, but
Inhibitory properties of low molecular mass cysteine proteinase inhibitors from human sarcoma.
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Elevated activities of cysteine proteinases such as cathepsins B and L and cancer procoagulant have been linked to tumor malignancy. In the present study we examined the hypothesis that these elevated activities could be due to impaired regulation by the endogenous low molecular mass cysteine
Enhanced levels of multicatalytic proteinase mRNAs in Rous sarcoma virus transformed cells.
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The multicatalytic proteinase (proteasome; MCP) is a high molecular mass proteinase which is found in all eukaryotic cells. Northern blot analysis of the levels of MCP mRNAs in a Rat-1 fibroblast cell line and in cells transformed with Rous sarcoma virus showed marked increases in the transformed
[Proteinases in the muscles of embryos and hens and and in transplantable muscle sarcoma].
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The authors examined the activity of acid proteinases in extracts, obtained by 0,05 M KCl from thigh muscles of 12-and 18-day hen embryos and of a 3-year hen and from muscle sarcoma 12--14 days after its transplantation on thigh muscles of a hen. The activity of the fractions obtained from extracts
Isolation and characterization of a trypsin-like serine proteinase from the membranes of Walker 256 carcino-sarcoma cells.
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A serine proteinase was isolated from Walker-256-carcino-sarcoma plasma-membrane-enriched preparations by affinity chromatography employing soya-bean trypsin inhibitor as the ligand. This enzyme was termed 'memsin' owing to its membrane location and trypsin-like substrate specificity. Analysis of
Purification and properties of extracellular matrix-degrading metallo-proteinase overproduced by Rous sarcoma virus-transformed rat liver cell line, and its identification as transin.
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Rous sarcoma virus-transformed rat liver cell line RSV-BRL secreted a neutral proteinase in a latent precursor form with a molecular weight (Mr) of 57,000 (57k) as a major secreted protein. This enzyme was a calcium-dependent metallo-proteinase. The proenzyme was purified from the serum-free
Transformation of rat liver cell line by Rous sarcoma virus causes loss of cell surface fibronectin, accompanied with secretion of metallo-proteinase that preferentially digests the fibronectin.
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An epithelial cell line derived from the liver of a normal Buffalo rat (BRL) was transformed by Rous sarcoma virus (RSV). The RSV-transformed cells were separated into five clones (RSV-BRL1 through 5), which were morphologically different. RSV-BRL cells exhibited the following characteristics
Cartilage-degrading neutral proteinase secreted by Yoshida sarcoma cells. Purification and properties.
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The Yoshida sarcoma, a malignant rat tumor, has been reported by Machinami ( Machinami , R. (1972) Acta Pathol. JPN 22, 19-39) to destroy cartilage matrix in vivo. We have characterized an enzyme secreted by Yoshida sarcoma cells in culture which degrades cartilage proteoglycan in solution and also
[Neutral proteinase of transplantable sarcoma tissue from rats].
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[Comparative study of rat sarcoma and liver acid proteinases. Functionally active groups].
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Localization of alpha 2-macroglobulin in human primary sarcomas and synthesis in established cell lines.
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The presence of alpha 2-macroglobulin (alpha 2M) was detected with the avidin-biotin technique in more than 20-yr-old paraffin blocks from human sarcomas. alpha 2M was found mainly in the cytoplasm of the tumor cells, and almost all tumor cells were positive. This serum glycoprotein, which is a
Kaposi's sarcoma-associated herpes virus complement control protein: KCP--complement inhibition and more.
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The complement system is an important part of innate immunity providing immediate protection against pathogens without a need for previous exposure, as well as priming the adaptive immune response through opsonisation, leukocyte recruitment and enhancing humoral immune responses. Its importance is
Isolation, biochemical characterization and crystallization of the p15gag proteinase of myeloblastosis associated virus expressed in E. coli.
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1. The p15gag proteinase responsible for the processing of the polyprotein precursor of the myeloblastosis associated virus was obtained by a recombinant technique in an E. coli expression system. The massive expression of the intentionally truncated precursor (Pr25lac-delta gag) was accompanied by
Cyclic AMP-dependent and -independent effects on tissue-type plasminogen activator activity in osteogenic sarcoma cells; evidence from phosphodiesterase inhibition and parathyroid hormone antagonists.
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The plasminogen activator (PA) in clonal osteogenic sarcoma cells of rat origin (UMR 106-01 and UMR 106-06) and in osteoblast-rich rat calvarial cells has been characterized using specific antibodies to be tissue-type PA (tPA). An Mr value of 75,000 by SDS-polyacrylamide gel electrophoresis and
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