Search Results - "Freedman, R.B."

Metabolic control of recombinant protein N-glycan processing in NS0 and CHO cells by Baker, Kym N., Rendall, Mark H., Hills, Anna E., Hoare, Michael, Freedman, Robert B., James, David C.

“…Chinese hamster ovary and murine myeloma NS0 cells are currently favored host cell types for the production of therapeutic recombinant proteins. In this study,…”
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Rapid monitoring of recombinant protein products: a comparison of current technologies by Baker, Kym N, Rendall, Mark H, Patel, Ashvin, Boyd, Paul, Hoare, Mike, Freedman, Robert B, James, David C

“…Specific measurement of recombinant protein titer in a complex environment during industrial bioprocessing has traditionally relied on labor-intensive and…”
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Fluorescence dynamics of staphylococcal nuclease in aqueous solution and reversed micelles by Visser, A J, van Engelen, J, Visser, N V, van Hoek, A, Hilhorst, R, Freedman, R B

“…The dynamical fluorescence properties of the sole tryptophan residue (Trp-140) in Staphylococcus aureus nuclease (EC 3.1.31.1) have been investigated in…”
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N-Glycosylation of Recombinant Human Interferon-γ Produced in Different Animal Expression Systems by James, David C, Freedman, Robert B, Hoare, Michael, Ogonah, Olotu W, Rooney, Barrie C, Larionov, Oleg A, Dobrovolsky, Vasily N, Lagutin, Oleg V, Jenkins, Nigel

“…Recombinant human interferon-gamma (IFN-gamma) was expressed in Chinese hamster ovary cells, baculovirus-infected Sf9 insect cells and the mammary gland of…”
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A comparison of lipase-catalysed ester and lactone synthesis in low-water systems: Analysis of optimum water activity by Alston, Mark J., Freedman, Robert B.

“…We investigated the effects of the lyophilisation medium (enzyme plus buffer salt and additives) and of water activity (aw) on the catalytic properties of…”
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The water-dependence of the catalytic activity of bilirubin oxidase suspensions in low-water systems by Alston, Mark J., Freedman, Robert B.

“…We investigated the enzymic activity of bilirubin oxidase when it is suspended as a lyophilized powder in a low‐water system. The enzyme required buffer salts…”
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A molecular model for the redox potential difference between thioredoxin and DsbA, based on electrostatics calculations by Gane, P.J., Freedman, R.B., Warwicker, J.

“…The disulphide active sites of thioredoxin and DsbA are known to possess a high degree of structural homology. However, DsbA is a much stronger oxidant than…”
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Mutations That Destabilize the a′ Domain of Human Protein-disulfide Isomerase Indirectly Affect Peptide Binding by Klappa, P., Koivunen, P., Pirneskoski, A., Karvonen, P., Ruddock, L.W., Kivirikko, K.I., Freedman, R.B.

“…Protein-disulfide isomerase (PDI) is a catalyst of folding of disulfide-bonded proteins and also a multifunctional polypeptide that acts as the β-subunit in…”
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Protein disulfide isomerase is essential for viability in Saccharomyces cerevisiae by Farquhar, R, Honey, N, Murant, S J, Bossier, P, Schultz, L, Montgomery, D, Ellis, R W, Freedman, R B, Tuite, M F

“…Protein disulfide isomerase (PDI) is an enzyme involved in the catalysis of disulfide bond formation in secretory and cell-surface proteins. Using an…”
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Comparison of the expression patterns of genes coding for wheat gluten proteins and proteins involved in the secretory pathway in developing caryopses of wheat by Grimwade, B. (Bristol Univ. (United Kingdom). Dept. of Agricultural Sciences), Tatham, A.S, Freedman, R.B, Shewry, P.R, Napier, J.A

“…The synthesis of gluten proteins in the developing caryopsis of wheat is highly coordinated, with mRNAs for the various groups being detected from 11 days…”
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High-resolution separation of recombinant human interferon-gamma glycoforms by micellar electrokinetic capillary chromatography by James, D C, Freedman, R B, Hoare, M, Jenkins, N

“…Recombinant human interferon-gamma (IFN-gamma) glycoform populations produced by Chinese hamster ovary cells have been resolved by micellar electrokinetic…”
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Assembly of the B subunit pentamer of Escherichia coli heat-labile enterotoxin: kinetics and molecular basis of rate-limiting steps in vitro. [Erratum: Oct 25, 1996, v. 271 (43), p. 27188.] by Ruddock, L.W, Coen, J.J.F, Cheesman, C, Freedman, R.B, Hirst, T.R

“…The B subunits of Escherichia coli heat-labile enterotoxin (EtxB) and cholera toxin (CtxB) assemble in vivo into exceptionally stable homopentameric complexes,…”
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Peptide binding to protein disulfide isomerase occurs at a site distinct from the active sites by NOIVA, R, FREEDMAN, R. B, LENNARZ, W. J

“…Protein disulfide isomerase (PDI) is a multifunctional protein resident in the lumen of the rough endoplasmic reticulum that facilitates protein folding via…”
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Protein disulfide-isomerase by Freedman, R B, Hawkins, H C, McLaughlin, S H

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Characterization of the subunits in an apparently homogeneous subpopulation of Clostridium thermocellum cellulosomes by Ali, Bassam R.S., Romaniec, Marek P.M., Hazlewood, Geoffrey P., Freedman, Robert B.

“…Clostridium thermocellum cellulosomes isolated by cellulose affinity chromatography were fractionated by anion exchange chromatography into apparently…”
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refolding of hen egg white riboflavin-binding protein: effect of protein disulphide isomerase on the reoxidation of the reduced protein by McClelland, D.A, McLaughlin, S.H, Freedman, R.B, Price, N.C

“…Hen egg white riboflavin-binding protein (RfBP) contains nine disulphide bonds. Provided these remain intact, the refolding of RfBP after incubation in 6 M…”
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Structural properties of homogeneous protein disulphide-isomerase from bovine liver purified by a rapid high-yielding procedure by Lambert, N, Freedman, R.B

“…Protein disulphide-isomerase from bovine liver was purified to homogeneity as judged by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis,…”
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Cloning and active site mutagenesis of Vibrio cholerae DsbA, a periplasmic enzyme that catalyzes disulfide bond formation by Yu, J, McLaughlin, S, Freedman, R B, Hirst, T R

“…Recently, a gene (dsbA) involved in the biogenesis of secreted oligomeric enterotoxins in Vibrio cholerae was described, which encodes an exported protein…”
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Using molecular genetics to improve the production of recombinant proteins by the yeast Saccharomyces cerevisiae by Schultz, L D, Markus, H Z, Hofmann, K J, Montgomery, D L, Dunwiddie, C T, Kniskern, P J, Freedman, R B, Ellis, R W, Tuite, M F

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Conformational differences between two wheat (Triticum aestivum) 'high-molecular-weight' glutenin subunits are due to a short region containing six amino acid differences by Goldsbrough, A.P, Bullied, N.J, Freedman, R.B, Flavell, R.B

“…'High-molecular-weight' (HMW, high-Mr) glutenin subunits are protein constituents of wheat (Triticum aestivum) seeds and are responsible in part for the…”
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