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  • 1
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 17 (1975), S. 465-479 
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The use of another air operated extreme pressure hydraulic pump fitted with either a needle valve or a simple microbore tube is described, together with the figures obtained for the soluble protein released from suspensions of commercially obtained baker's yeast (Saccharomyces cerevisiae). The theory of the mechanism is also discussed.
    Additional Material: 9 Ill.
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  • 2
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 17 (1975), S. 1065-1081 
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The dynamics of a system of two microbial populations having complementary metabolism are investigated by means of simple mathematical models of growth. Complementary metabolism as used here means that each population produces a substance - not present in the initial or feed medium - required by the other for growth. The simple models indicate that (1) something other than lack of the substrate or growth factor produced by its partner must limit the growth of at least one population and (2) the coexistence steady state of such populations in continuous culture is not stable with respect to large perturbations, though it is stable with respect to a wide range of perturbations.
    Additional Material: 9 Ill.
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  • 3
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Additional Material: 6 Ill.
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  • 4
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 46 (1995), S. 333-342 
    ISSN: 0006-3592
    Keywords: biodegradation ; chlorinated hydrocarbons ; trichloroethylene ; microbial kinetics ; chemostat ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Microbial degradation of trichloroethylene (TCE) has been demonstrated under aerobic conditions with propane. The primary objective of this research was to evaluate the feasibility of introducing a vapor phase form of TCE in the presence of propane to batch bioreactors containing a liquid phase suspension of Mycobacterium vaccae JOB5 to accomplish degradation. The reactor system consisted of three phases: a vapor phase introducing air, propane, and TCE; a liquid phase of the microbial suspension; and a solid phase in the form of the microorganisms. Long-term and initial rate experiments were conducted on three culture sets to evaluate microbial response. In two long-term test fed propane and approximately 0.1 mg/L and 1 mg/L of TCE, respectively, propane utilization was more efficient at the high TCE concentration (600 mmol propane/mmol TCE versus 11,900 mmol propane/mmol TCE), because the propane degradation rate was approximately the same for both tests (6.73 mg/L · h and 7.85 mg/L · h for the high and low tests). In addition, TCE utilization decreased after complete propane consumption. Initial rate tests on culture sets fed propane only revealed that cells with a history of exposure to a high concentration of TCE had the highest specific growth rate, but the lowest half-saturation constant (7.60e-3 h-1 and 0.10 mg/L, respectively). Tests fed variable TCE concentrations (0.031 to 5.378 mg/L in the liquid phase) with no propane showed TCE depletion but no biomass growth. The tests revealed that the TCE removal increased as the TCE concentration increased, indicating a greater removal efficiency at the higher concentrations. Tests with a constant initial propane concentration and variable liquid phase TCE concentration revealed that specific propane utilization was essentially the same. © 1995 John Wiley & Sons, Inc.
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  • 5
    Electronic Resource
    Electronic Resource
    Weinheim : Wiley-Blackwell
    Electrophoresis 19 (1998), S. 2133-2139 
    ISSN: 0173-0835
    Keywords: Sea water ; Capillary electrophoresis ; High salt concentrations ; Anion analysis ; Joule heating ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: It is commonly thought that even a moderately high ionic concentration in the background electrolyte (BGE) would leaad to Joule heating and serious peak distortion. However, we obtained very satisfactory separations of both inorganic and organic anions in electrolyte solutions as high as 5 M sodium chloride using direct photometric detection. Samples containing a 0.5 M concentration of a salt can be analyzed directly by making the BGE concentration of the same salt even higher to obtain electrostacking. The temperature in the center of the capillary was calculated to be 49°C when the current is at its maximum of 280 μA. The effect of various salts on electrophoretic and electroosmotic mobility is discussed. Several examples are given of capillary electrophoresis under high-salt conditions.
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  • 6
    ISSN: 0173-0835
    Keywords: Two-dimensional polyacrylamide gel electrophoresis ; Mass spectrometry ; Peptide mass fingerprinting ; Capillary liquid chromatography ; Human colonic proteins ; Immunoblot analysis ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Immunochemical detection of proteins with antigenic determinants that are dependent on the native spatial conformation of the protein can often pose problems with conventional two-dimensional polyacrylamide gel electrophoresis (2-DE). For example, many antigenic determinants are readily destroyed by reducing agents and/or urea, reagents which are critical components of many of the conventional isoelectric focusing and immobilized-pH-gradient (IPG) protocols used in the first electrophoretic dimension. Here we describe the use of commercially available precast 2-DE gels for performing nonreducing/non-urea 2-DE of proteins extracted from the human colon cancer cell line LIM 1215 with 0.3% Triton X-100 that permit the identification of antigens with conformational determinants by immunoblot analysis. Previous, related studies demonstrated the usefulness of peptide-mass fingerprinting for identifying 2-DE resolved proteins. Here we show how partial protein sequence data obtained by rapid peptide mapping, using capillary column liquid chromatography directly coupled with electrospray ionization tandem mass spectrometric methodologies, enhances the usefulness of this approach for identifying incompletely resolved proteins. The nonreducing 2-DE gel images reported in this study, along with our master 2-DE gel protein database for both normal human colonic crypts and several colon-cancer-derived cell lines, and information regarding microtechniques employed in this laboratory for obtaining structural data on 2-DE resolved proteins can be accessed over the Internet using World Wide Web (URL address: http://www.ludwig.edu.au).
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  • 7
    ISSN: 0173-0835
    Keywords: Two-dimensional polyacrylamide gel electrophoresis ; Human breast carcinoma proteins ; Tandem mass spectrometry ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Previously, we reported a two-dimensional gel map and database with molecular weight/isoelectric point (Mr/pI) loci for 22 proteins expressed in the breast carcinoma cell line, MDA-MB231 (Rasmussen et al., Electrophoresis 1997, 18, 588-598). Here we update this database with Mr/pI loci for a further nine cytoplasmic proteins and three Triton X-114 solubilised membrane proteins from MDA-MB231 cells. In addition, a novel protein, previously represented only in expressed sequence tag (EST) databases, has been identified as a Triton X-114 soluble protein and assigned an Mr/pI locus. During the course of isolating proteins from the Triton X-114 fraction, we compared recoveries of proteins in sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) gels after isoelectric focusing (IEF) using either immobilised pH gradients or carrier ampholytes. In these experiments, a significantly higher proportion of membrane proteins were visible in SDS-polyacrylamide gels after the use of carrier ampholytes for the first dimension. We also report our mass spectrometric-based procedure for identifying two-dimensional electrophoresis (2-DE) gel-resolved proteins, combining in-gel enzymatic digestion, 0.2 mm internal diameter (ID) capillary column reversed-phase high-performance liquid chromatography (RP-HPLC) peptide mapping and electrospray ionisation  -  ion trap  -  mass spectrometry.
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  • 8
    ISSN: 0173-0835
    Keywords: MLK2 ; Mixed lineage kinase ; SH3 domain ; Protein identification ; Two-dimensional polyacrylamide gel electrophoresis ; Mass spectrometry ; Human breast carcinoma cell line ; β-Tubulin ; Prohibitin ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: The mixed lineage kinase 2 (MLK2) protein contains several structurally distinct domains including an src homology (SH) 3 domain, a kinase catalytic domain, two leucine zippers, a basic motif and a cdc42/rac interactive binding motif. These domains have been recognized mainly for their involvement in protein-protein interactions in signal transduction networks. The SH3 domain in particular has been implicated in control of signaling events. To identify proteins that interact with MLK2, the N-terminal 100 amino acids, including the SH3 domain, were expressed as a glutathione S-transferase (GST) fusion protein. This fusion protein (MLK2N) was used as an affinity ligand to isolate binding proteins from lysates of 35S-radiolabeled MDA-MB231 breast carcinoma cells. When the radiolabeled binding proteins were subjected to 2-DE, proteins of Mr 55 000, 31 500 and 34 000 bound consistently to the MLK2N domain fusion protein, but not to the GST control. Two of the binding proteins were isolated from whole cell lysates by preparative 2-DE and subjected to in-gel digestion and capillary or microbore reverse-phase high performance liquid chromatography (RP-HPLC). Resultant peptides were analyzed by peptide masss fingerprinting, N-terminal Edman degradation or tandem mass spectrometry. The 55 000 protein was identified as the cytoskeletal protein, β-tubulin, and this was verified by immunoblotting of proteins in the MLK2N binding fraction with anti-tubulin antibodies. The 31 500 protein has been identified as prohibitin, a protein that has been implicated in both signal transduction and cell cycle arrest.
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  • 9
    ISSN: 0173-0835
    Keywords: Two-dimensional gel polyacrylamide gel electrophoresis ; Mass spectrometry ; Peptide mass fingerprinting ; Capillary liquid chromatography ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: In-gel proteolytic digestion of acrylamide-gel separated proteins is a method widely used for generating peptide fragments for the purpose of identifying proteins by Edman degratation, tandem mass spectrometry, and peptide-mass fingerprinting. However, it is well recognised for disulfide-bonded proteins electrophoresed under reducing conditions that if no precautions are taken to minimise disulfide bond formation during protein digestion or peptide isolation, complex peptide maps can result. Here, we describe an improved method for in-gel protein digestion. It consists of first reducing and S-pyridylethylating Coomassie Brilliant Blue R-250-stained proteins immobilised in the whole gel slab with dithiothreitol and 4-vinylpyridine, excising the individual stained and alkylated proteins, and then digesting them in situ in the gel matrix with trypsin or Achromobacter lyticus protease I. Peptide fragments generated in this manner are extracted from the gel piece and purified to homogeneity by a rapid (≤12 min) reversed-phase high performance liquid chromatography (HPLC) procedure, based upon conventional silica supports. Recoveries of peptides are increased by S-pyridylethylation of acrylamide-immbilised proteins prior to in-gel digestion. Further, the levels of gel-related contaminants, which otherwise result in suppression of sample signals during electrosprayionisation mass spectrometry, are greatly reduced by the reduction / alkylation step. Additionally, we demonstrate that S-β-(4-pyridylethyl)-cysteine containing peptides can be readily identified during reversed-phase HPLC by absorance at 254 nm, and during electrospray ionisation tandem mass spectrometry by the appearance of a characteristic-pyridylethyl fragment ion of 106 Da. The position of cysteine residues in a sequence can be determined as phenylthiohydantoin S-β-(4-pyridylethyl)-cysteine during Edman degradation, and by tandem mass spectrometry.
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  • 10
    ISSN: 0173-0835
    Keywords: Two-dimensional polyacrylamide gel electrophoresis ; Tandem mass spectrometry ; Peptide mass fingerprinting ; Post-source-decay fragmentation ; Human colonic proteins ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: The master two-dimensional gel database of human colon carcinoma cells currently lists cellular proteins from normal crypts and the colorectal cancer cell lines LIM 1863, LIM 1215 and LIM 1899 (Ward et al., Electrophoresis 1990, 11, 883-891; Ji et al., Electrophoresis 1994, 15, 391-405). Updated two-dimensional electrophoretic (2-DE) maps of cellular proteins from LIM 1215 cells, acquired under both nonreducing and reducing conditions, are presented. Fifteen cellular proteins are identified in the reducing 2-DE gel map, and seven in the nonreducing gel map, along with a tabular listing of their Mr/pI loci and mode of identification. We also include our mass spectrometric based procedures for identifying 2-DE resolved proteins. This procedure relies on a combination of capillary column (0.10-0.32 mm internal diameter) reversed-phase HPLC peptide mapping of in-gel digested proteins, peptide mass fingerprinting, sequence analysis by either collision-induced dissociation or post-source-decay fragmentation, and protein identification using available database search algorithms. These data, and descriptions of the micro-techniques employed in this laboratory for identifying 2-DE resolved proteins can be accessed via the internet URL: http://www.ludwig.edu.au.
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