Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0027651 (tumor)
 685,946 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

For the purification and further characterisation of the skin-reactive factor (SRF) of the mouse, the SRF-containing ascitic fluid of Ehrlich ascites tumor was exposed to different separation or elution procedures. After preliminary purification by (NH4)2SO4 precipitation when the total activity was not in the dialysable supernatant, gel-chromatographic separation (Sephadex G-200), immune electrophoretic investigations as well as ion exchange chromatography were performed. The skin-reactive activity in fraction I of gel chromatiography is presumably caused by a toxic substance with skin-irritating properties. The SRF demonstrable in fraction II/2 has a molecular weight similar to that of albumin, can be found in the ion exchange chromatography (DEAE-Sephadex A-50-column) in fraction III, and is of proteinic nature.
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PMID:[Purification of skin reactive factor (SRF) in mice]. 13 6

The mucopolysaccharides were prepared from human lung carcinomas of three histologically different types and the control tissue by exhaustive proteolytic digestion, quaternary ammonium chloride fractionation and column chromatography on Dowex 1 (Cl-). They were identified by chemical, enzymic and electrophoretic methods, as hyaluronic acid (HA), chondroitin sulfate (ChS), dermatan sulfate (DS), heparan sulfate (HS) and over-sulfated ChS and/or DS. Qualitatively they were not differed in tumor and normal tissues. However, the amounts of whole mucopolysaccharide were much increased in carcinomas than those of normal control in order of squamous cell carcinoma greater than small cell undifferentiated carcinoma greater than or equal to adenocarcinoma. The increment of mucopolysaccharide contents in carcinoma are largely due to increased amounts of HA and ChS. Carcinoma-type characteristic pattern was also demonstrated in terms of relative amounts of non-sulfated (HA) and sulfated (ChS, DS, HS) mucopolysaccharides: In squamous cell carcinoma and adenocarcinoma sulfated mucopolysaccharides were predominant (73 to 78% of total mucopolysaccharides), whereas in small cell undifferentiated carcinoma sulfated ones were diminished (25% of total mucopolysaccharides). In normal lung tissue sulfated mucopolysaccharide comprised 64% of total mucopolysaccharides. The presence of over-sulfated ChS and/or DS, which have not until now been found in lung tissue, was higher in carcinoma tissue as compared to the normal control. Total glycopeptides which were derived from tissue glycoproteins and not in detail characterized in this study were decreased in carcinomas of any histological types as compared to those of normal lung tissue, when expressed by hexosamine content. Biological and clinical significance of mucopolysaccharides in carcinoma state was discussed.
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PMID:[Study on mucopolysaccharides in human lung carcinoma tissue--characteristics in histological types (author's transl)]. 16 61

DNA-dependent RNA polymerases were extracted from the nuclei of poorly differentiated tumor, Morris hepatoma 3924A, and purified by an initial chromatography on a DEAE-Sephadex column followed by fractionation on phosphocellulose and finally on a second DEAE-Sephadex column. Three major forms of RNA polymerase (IA, IB and II) were resolved chromatographically. Enzymes IA, IB and II eluted from DEAE-Sephadex at 75, 150 and 210 mM (NH4)2SO4, respectively. The specific activities (nmol UMP incorporated mg protein per 15 min) of polymerases IA, IB and II were 40, 43 and 182, respectively. Concurrently, DNA-dependent RNA polymerases were extracted from normal liver and subjected to similar chromatographic procedure. Upon the final DEAE-Sephadex chromatography, enzymes IA, IB and II eluted at 110, 180 and 210 mM (NH4)2SO4, respectively. The recovery of polymerases IA, IB and II after purification was 0.21, 0,28 and 0.42 unit/mg DNA, respectively, for hepatoma enzymes and 0.07, 0.05 and 0.42 unit/mg DNA for the corresponding liver enzymes.
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PMID:RNA polymerases from a rat hepatoma. Partial purification and comparison of properties with corresponding liver enzymes. 17 77

The activity of purified RNA polymerase II from Novikoff ascites tumor cells is stimulated 5-7-fold by a purified protein factor. This protein factor, designated HLF2, has extensive protein kinase activity and catalyzed the incorporation of gamma-32G from ATP into protein under normal RNA polymerase assay conditions. Protein phosphorylation is totally dependent on the presence of HLF2 and is stimulated 2-3-fold by the presence of highly purified RNA polymerase II. The purification procedure developed for the isolation of the polymerase stimulatory factor resulted in a 4000-fold purification of a protein kinase. Chromatography on carboxymethylcellulose, phosphocellulose, and Sephadex G-100 did not resolve polymerase stimulatory activity from protein kinase activity. Adenylimidodiphosphate (AMP-PNP), an inhibitor of protein kinases, inhibited the stimulatory activity of purified factor by 80%. The heat denaturation profile of protein kinase was paralleled by the loss of polymerase stimulatory activity. Concentrations of (NH4)2SO4 which are known to inhibit polymerase stimulation (Lee and Dahmus, 1973) also inhibit protein kinase activity. The protein kinase activity associated with stimulatory factor catalyzes the phosphorylation of basic proteins such as protamine or histone. The protein kinase is not stimulated by cyclic 3', 5'-AMP or -GMP over a concentration range of 10(-6)-10(-4)M. Furthermore, protein kinase activity is not inhibited by either the regulatory subunit of rabbit muscle protein kinase or by the heat-stable inhibitor of cyclic 3', 5'-AMP-dependent protein kinases. Protein kinase activity is stimulated by KCl or NH4Cl and is inhibited by MnCl2. The apparent Km values, determined in the presence of 4 mM Mg2+, are 0.02 mM for ATP, and 4.1 mM for GTP.
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PMID:Stimulation of ascites tumor RNA polymerase II by protein kinase. 17 56

In order to demonstrate a collagenolytic enzyme in a tumor, solid Tawa sarcoma was subjected to a tissue culture technique. Salt- and acid-soluble collagen used as substrate was extracted from the rat skin and tail tendon. The tumor mass used was obtained on the 5th, 8th, and 11th days after subcutaneous transplantation of ascites Tawa sarcoma cells. Each tissue fragment in the inner and outer layers of the tumor mass was incubated on collagen gel at 37 degrees for 4 days, and collagenolytic activity was determined by comparing the relative content of hydroxyproline in the attacked collagen which was separated by means of centrifugation. All fragments were found to possess collagenolytic activity with some variation. Higher activity was observed in the outer layer than in the inner layer. Tumor fragments were cultured, and the collagenolytic enzyme was isolated from the culture medium and concentrated by ammonium sulfate precipitation and acrylamide disc electrophoresis. Collagenolytic enzyme activity was examined for its mode of attack on native collagen.
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PMID:Collagenolytic enzyme in solid Tawa sarcoma. 17 66

A solubilization technique employing 0.5% Triton X-100 was developed to obtain both SV40 virus (SV40)-induced tumor-specific surface antigen(s) (TSSA) from SV40-transformed mouse cells, as determined by a serum-mediated microcytolytic assay, and tumor-specific transplantation antigen(s) (TSTA), as determined by in invivo experiments. High yields (approximately 50%) of TSSA were obtained in whole-cell extracts and also after ammonium sulfate fractionation. Additional fractionation of a 30-50% ammonium sulfate fraction by gel exclusion chromatography on Sephadex G-150 resulted in two pooled fractions which contained TSSA activity. The first eluted close to the void volume, and the second in the 45,000 molecular weight region. The various TSSA active fractions were also active in vivo TSTA tests. Detergent solubilization provides a suitable technique to recover the SV40-induced antigens in good yield, and apparently in intact form.
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PMID:Detergent solubilization and partial purification of tumor specific surface and transplantation antigens from SV40-virus-transformed mouse cells. 19 Jan 77

Surface antigens were extracted in soluble and active form with 3 M KCL from polyoma virus-transformed and embryonic hamster cells. These were tumor-specific transplantation antigens (TSTA), shown by tumor rejection, and a surface (S) antigen, demonstrated by the inhibition of surface fluorescence on living polyoma virus-transformed cells. The extracts were fractionated by salting out with ammonium sulfate. In tumor cell extracts, all TSTA activity and a part of S antigen activity were found in the fraction precipitated with 60% saturation in (NH/)2SO4. Another part of S antigen activity was found in the fraction precipitating at 80% saturation in tumor cell extracts. The precipitate at 60% saturation of embryonic cell extracts also had a part of S antigen activity. Receptor site activity for concanavalin A was also retained after solubilization and was confined to the 40% saturation (NH4)2SO4 precipitate in the case of tumor and embryonic cell extracts.
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PMID:Isolation of polyoma virus-induced surface antigens in hamster cells: potassium chloride solubilization and differential precipitation. 19 Apr 15

Previous studies with isolated adrenocortical carcinoma 494 cells from this laboratory have indicated that the lack of cyclic adenosine 3':5'-monophosphate (cyclic AMP) control in steroidogenesis in the tumor may be due to the defective cyclic AMP-dependent protein kinase enzyme system. This paper describes the partial purification of such an enzyme. Purification was achieved by precipitation of the tumor homogenate with 30 and 45% ammonium sulfate, adsorption on 3% calcium phosphate gel, and chromatography on DEAE-cellulose. Four major protein peaks were isolated. Peak 2 showed cyclic AMP-binding activity and was investigated further for its kinetic properties. In contrast to the cyclic AMP-dependent protein kinase enzyme found in the normal adrenal gland, the enzyme specifically bound cyclic AMP but failed to phosphorylate exogenous histone. It is postulated that lack of the cyclic nucleotide-dependent kinase activity of the protein kinase enzyme may be responsible for the loss of cyclic AMP-regulated corticosterone synthesis in adrenocortical carcinoma cell. It is further shown that the tumor cyclic AMP-binding enzyme undergoes endogenous phosphorylation, which indicates that it has kinase activity but it is independent of cyclic AMP.
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PMID:Partial purification and characterization of the defective cyclic adenosine 3':5'-monophosphate binding protein kinase from adrenocortical carcinoma. 19 24

SV40 T-antigen was isolated from hamster tumors and purified about 1600-fold by the procedure including successive ammonium sulfate precipitation, chromatography on DEAE-cellulose, preparative polyacrylamide gel electrophoresis and elimination of the bulk of contaminating cell proteins by the interaction with antibodies to the tissues of normal hamsters. The resulting preparation was not quite homogenous being contaminated with some of cell proteins left. T-antigen in the tumor extract was revealed at least in three distinct forms with molecular weight of 100 000, 200 000, and 400 000. It is proposed that these forms correspond to mono-, di-, and tetramers of the basal protein of T-antigen, although the alternative explanation, the existence of complex of T-antigen with cell proteins, cannot be ruled out.
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PMID:[Preparative isolation and some properties of SV40 T-antigen]. 19 85

The simian virus 40 (sv40) tumor antigen (T-antigen) and tumor-specific transplantation antigen (TSTA) have been partially purified and studied to clarify their relationship. The T-antigen and the TSTA were partially purified from nuclei of SV AL/N cells, and SV40-transformed mouse embryo fibroblast line, by precipitation with ammonium sulfate and chromatography on DEAE- and DNA-cellulose. The T-antigen was assayed by complement fixation, and the TSTA was assayed by its ability to immunize mice against SV40-containing ascites tumor cells. When T-antigen- and TSTA-containing preparations were sedimented through sucrose gradients, each antigen had a major peak of activity at a sedimentation coefficient of 6.7 and minor peaks in other regions. Antiserum against T-antigen (from tumor-bearing hamsters) immunoprecipitated the TSTA activity. A preparation of T-antigen from human SV80 cells, which exhibited only one protein band after sodium dodecylsulfate-polyacrylamide gel electrophoresis, had TSTA activity when as little as 0.6 microgram of protein per mouse was used for immunization. These experiments demonstrate that the T-antigen, the product of the SV40 early A gene is capable of inducing specific immunity against transplantation of SV40-transformed tumor cells in mice.
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PMID:Relationship between T-antigen and tumor-specific transplantation antigen in simian virus 40-transformed cells. 21 35


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