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Query: UMLS:C0272170 (SDS)
 50,377 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Polypeptide growth factor isolated from bovine platelets was classified on the basis of its physico-chemical and biological properties to be transforming growth factor type beta (TGF beta). This growth factor was completely purified from platelet lysate by acid ethanol extraction, Bio-Gel P-60 filtration, ion-exchange chromatography on CM-Sephadex followed by two successive gel filtrations on Bio-Gel P-10 and Sephadex G-100. After the last gel filtration over 35,000-fold purified TGF beta was obtained. The purity of the preparation was confirmed by SDS-polyacrylamide gel electrophoresis, which revealed a single protein band with Mr of 25,000-27,000. Further studies showed that native TGF beta consists of two Mr 13,000 polypeptide chains held together by disulfide bonds.
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PMID:Bovine transforming growth factor beta. Purification and characterization. 248 81

Newer developments in molecular biology offer the hospital epidemiologist and clinical microbiologist powerful tools for analysis of nosocomial epidemics. Plasmid fingerprinting and genomic REA are rapid and often more definitive alternatives to serotyping and biotyping. Isolation of specific plasmids for special study involves more complicated manipulations. Polypeptide patterns, though at times diffuse in appearance, can be easily produced with SDS-PAGE of whole cells or outer membranes. Specific monoclonal antibodies as probes for individual proteins can generate more definitive answers about the exact type of protein(s) present. Multilocus enzyme electrophoresis (MLE) has become an ingenious tool for characterizing closely related nosocomial bacterial strains. The newest molecular methods using ribotyping, DNA probes, and the PCR will open many doors into the microbial genomes that were previously closed to the hospital microbial detective. These advances will compel hospitals to plan for their funding and implementation. Yet, like other scientific progress, the new biology in the nosocomial setting will raise as many questions as it will answer.
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PMID:Molecular analysis of nosocomial epidemics. 251 43

Polypeptide and Western immunoblot profiles of subcellular fractions of Treponema denticola ATCC 33520 have been determined by SDS-PAGE of Triton X-100-soluble and -insoluble fractions, a lipopolysaccharide-enriched fraction and purified flagella. Major Triton X-100-soluble polypeptides of 72, 68, 54 and 52 kDa were detected. The 54 kDa polypeptide appeared to be a breakdown product of a larger, heat-modifiable polypeptide. Based on the results of SDS-PAGE analysis and immunoblotting of proteinase K digests of T. denticola, a 'rough' lipopolysaccharide appeared to be present. Electron microscopy has been used to monitor the effect of detergent treatment on the morphology of the organism and to examine the detailed structure of the flagella. Treatment with Triton removed the T. denticola outer membrane, resulting in exposure of the flagella. The flagella were shown to have a complex sheath and core structure and polypeptide composition characteristic of that observed for other treponemes. Polypeptides of 38, 35, 32 and 28 kDa were present in purified flagella preparations. Immunoelectron microscopy, iodine-labelling and Western blotting were used to demonstrate the exposure of antigens on the T. denticola surface. Surface iodination located polypeptides of 72, 68 and 54 kDa. Antiserum raised against whole cells of T. denticola recognized these polypeptides and an additional polypeptide of 52 kDa. These data provide a basis for future detailed molecular analysis of the ultrastructure and antigenicity of T. denticola.
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PMID:Antigenic and structural analysis of Treponema denticola. 263 57

The polypeptides associated with fowlpox virus (FPV) infection of chicken embryo skin (CES) cells were examined by metabolic labelling with [35S]-methionine and sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). Polypeptide synthesis was followed over the first 48 hours post infection, as this was shown to be the period of viable virus production in CES cells. In contrast to infection with vaccinia virus (VV), which leads to a rapid total inhibition of host polypeptide synthesis in a number of cell lines, FPV infection of CES cells failed to cause a complete shut down of host polypeptide synthesis, with only a small number of host polypeptides being inhibited. A total of 21 FPV coded or induced polypeptides were resolved by metabolic labelling. As with VV, these polypeptides can be divided into two groups, the pre-replicative polypeptides containing a single member of 70,000 daltons, synthesised before viral DNA replication, and the post-replicative polypeptides, synthesised only after viral DNA replication has commenced. FPV DNA replication was shown to commence between 12 and 16 hours post-infection and to continue up to 48 hours post-infection. As also observed with VV, two temporally distinct classes of post-replicative polypeptides were identified based on their time of synthesis post-infection. The examination of purified FPV and VV by SDS-PAGE and coomassie blue staining allowed the resolution of 57 FPV particle associated polypeptides and 27 VV associated polypeptides.
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PMID:Fowlpox virus polypeptides: sequential appearance and virion associated polypeptides. 282 60

We have compared several aspects of an aphthovirus strain attenuated for cattle (C3R-O/E) with the original strain (C3Res) from which it was derived after serial passages in chicken embryos. Biochemical differences detected by protein analysis in regular polyacrylamide gels (SDS-PAGE) and on electrofocusing gels (NEPHGE) suggest the presence of mutations throughout the genome. Changes were located in coat proteins VP1 and VP3 and in the polymerase precursor P100 (P3/ABCD). No other differences were found at the protein level by means of the techniques used. Polypeptide P100 of the attenuated strain showed a faster electrophoretic mobility in SDS-PAGE with respect to that of the wild-type strain, and the change seems to be located on its amino terminus half. Several functional differences were also found between the two viruses. Both strains grew equally well in BHK cells reaching roughly similar titers in plaque assays. However, the wild-type strain maintained its titer in cells of bovine origin (BK), whereas the titer of C3R-O/E strain decreased approximately one log in this cell system; moreover, plaques elicited by the attenuated strain were much smaller than the ones produced by C3Res. A diminution in the rate of RNA synthesis induced by C3R-O/E in BK cells compared with that of the wild-type strain was also detected; this trait was not observed in BHK cells. A delay in the kinetics of RNA synthesis was also detected in this strain. The virus yield of attenuated strain in BK cells was four times lower than in BHK cells.
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PMID:Biochemical characterization of an aphthovirus type C3 strain Resende attenuated for cattle by serial passages in chicken embryos. 302 77

Antisera against synthetic peptides corresponding to various regions of the Main Intrinsic Polypeptide (MIP26K) of fiber lens membranes have been used to probe Western blots of Emory mouse lens proteins resolved by SDS-polyacrylamide gel electrophresis. When compared with clear lenses from control animals of approximately the same age, the MIP26K component from Emory mouse lenses demonstrated no quantitative changes in the binding of anti-MIP26K256-263 and anti-MIP26Kwhole sera. In contrast, the MIP26K component from Emory mouse lenses bound significantly better to two other antisera directly against other parts of the molecule (antiMIP26K229-237 and anti-MIP26K252-259). Furthermore, this increase in binding was approximately proportional to the degree of lens opacification. Together, these results demonstrate that during the opacification process of the Emory mouse lens, there occur covalent changes in the MIP26K molecule that, in part, may mimic those occurring in the human senile cataract.
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PMID:Changes in the major intrinsic polypeptide (MIP26K) during opacification of the Emory mouse lens. 304 12

Polypeptide constituents of the lens glucose transporter have been identified by photoaffinity labelling with cytochalasin B. The urea-insoluble fraction of monkey lens was irradiated at 280 nm for 30 min in the presence of 5 X 10(-7) M 3H-cytochalasin B. After extensive washing, the membranes were solubilized and their polypeptide composition determined by SDS-PAGE. Radioactivity was extracted from gel slices to determine the position of photoincorporated label. 3H-cytochalasin B was irreversibly incorporated into a broad molecular weight region from Mr greater than 94,000 to 43,000 with the peak of activity occurring at Mr 53,000. Photoincorporation was inhibited by D-glucose (500 mM) and phloretin (1 X 10(-5] but was unaffected by L-glucose (500 mM), cytochalasin E (1 X 10(-5) and phloridzin (1 X 10(-5) M). Cortex and nucleus membrane preparations contained the same range of labelled polypeptides after photoaffinity labelling but nuclear membranes contained approximately twice the activity of cortical membranes indicating an enrichment of glucose transporters in the nucleus. Treatment of labelled membranes with endoglycosidase F converted the broad band of labelling to a sharp band of Mr 45,000. The lens glucose transporter is therefore a glycoprotein and the broadness of the photaffinity labelled peak is due to heterogeneous N-linked glycosylation of a core polypeptide. From these studies it appears that the monkey lens glucose transporter closely resembles that of the human erythrocyte.
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PMID:Identification of the monkey lens glucose transporter by photoaffinity labelling with cytochalasin B. 312 91

Polypeptide transforming growth factors: TGF alpha and TGF beta were isolated and separated from acidic ethanol extracts of mouse C-243 tumors. The purification of the acid-soluble extract was achieved by Bio-Gel P-60 filtration chromatography, followed by CM-Sepharose CL-6B ion exchange, Bio-Gel P-10 filtration, and dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). At the Bio-Gel P-10 purification step, TGF alpha was separated from TGF beta. TGF alpha stimulated mouse Balb/c-3T3, rat NRK-49F and human A549 cells to form colonies in soft agar, and competed with 125I-labeled epidermal growth factor (EGF) for binding to human placenta membrane receptors. Over 40,000-fold SDS-PAGE-purified TGF beta had an Mr of 25,000. Unlike TGF alpha, TGF beta stimulated the clonal growth of NRK fibroblasts only in the presence of the suboptimal amounts of EGF (0.5 ng/ml). TGF beta significantly inhibited the anchorage-independent growth of malignant human lung carcinoma A549 cells, and in the radioreceptor assay with 125I-EGF it had no affinity to EGF receptors.
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PMID:Separation of transforming growth factors TGF alpha and TGF beta during chromatographic purification of extracts from mouse C-234 tumors. 350 41

Enriched gonadotrophs from rat pituitaries were used to analyze the kinetics of release in vitro of the Gonadotrop Polypeptide (GP-87) under LHRH stimulation. Proteins in cultured cells were labeled with [35S]methionine. Labeling of the intracellular GP-87 pool was effected during 16 hours prior to LHRH (10(-7) M) stimulation. Proteins were analyzed either by one-dimensional SDS-PAGE (Medium content) or by two-dimensional PAGE (Cell content). An apparent half-life (intracellular catabolism + release) of 31 h for GP-87 was estimated from control cells; it dropped to 2.5 h in stimulated cells due to intense release (26% after 1 h and about 80% after 8 h of stimulation). When cells were simultaneously labeled and stimulated, the newly synthesized species appeared in the medium after a lag phase of 30 minutes, time required for synthesis and full subsequent processing. From both series of experiments, it is concluded that the hypothalamic decapeptide promotes exocytosis of the newly synthesized GP-87 well before the endogenous GP-87 pool is exhausted. Furthermore, the release of another discrete protein (B2, Mr: 81 kDa) is also stimulated by LHRH. These proteins being co-released with LH could be part of the sorting and/or routing process of hormones towards exocytosis.
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PMID:LHRH-stimulated release of stored and newly synthesized gonadotrop polypeptide (GP-87) by cultured rat gonadotrophs. 355 81

Polysomes from rabbit endometrium, incubated in a cell-free system in the presence of [35S]methionine, completed polypeptide chains pre-initiated in vivo. Polypeptide chains were analyzed by SDS-gel electrophoresis after immunoprecipitation with anti-uteroglobin. Endometrial polysomes, freed of membranes by detergent treatment, synthesized both mature uteroglobin and preuteroglobin not yet cleaved in vivo. Membrane-bound polysomes synthesized exclusively mature uteroglobin, indicating the processing of preuteroglobin by the membranes bound to the ribosomes.
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PMID:Cell-free synthesis of preuteroglobin and processing to uteroglobin by polysomes from rabbit endometrium. 389 54


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