Library

feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    ISSN: 1520-6882
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 2
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Biotechnology progress 10 (1994), S. 433-440 
    ISSN: 1520-6033
    Source: ACS Legacy Archives
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 3
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 48 (1995), S. 25-35 
    ISSN: 0006-3592
    Keywords: DNA purification ; DNA-binding fluorophore ; Fluorescent ligand ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The fluorescent probe PO-PRO-3 was investigated as a potential ligand for the affinity immobilization and purification of genomic or plasmid DNA fragments. Affinities and mechanisms for PO-PRO-3 binding to superhelical and linearized pUC 18 plasmid DNA were examined through measurement of binding isotherms, continuous-variation analysis, and DNA titrations. In addition, the effects of DNA conformation, protein and RNA contaminants, solvent polarity, and ionic strength are examined with the aim of optimizing binding and elution conditions and of assisgning limits to the range of applicability of the affinity purification. © 1995 John Wiley & Sons, Inc.
    Additional Material: 11 Ill.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 4
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 46 (1995), S. 185-193 
    ISSN: 0006-3592
    Keywords: image analysis ; cell attachment ; mammalian cells ; cellulase ; Cellulomonas fimi ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: A luminance thresholding procedure was developed to quantify cell attachment of a variety of cell lines to CBD/RGD, a hybrid attachment factor comprising a cellulose binding domain and the fibronectin-like RGD attachment peptide. The technique used local thresholding, median filtering, and opening to separate and count cells on each image. Cell lines exhibited three different patterns of attachment to CBD/RGD, depending on whether it was immobilized on polystyrene or cellulose acetate. Vero, COS, HFF, 3T3, 293, and U373 cells attached well to CBD/RGD immobilized on polystyrene or cellulose acetate. CHO, MRC-5, and HEp-2 cells attached to CBD/RGD immobilized on polystyrene, but not to CBD/RGD immobilized on cellulose acetate. BHK and L cells failed to attach to CBD/RGD immobilized on either polystyrene or cellulose acetate. The attachment of many cell lines to CBD/RGD was comparable with attachment of these cells to fibronectin. © 1995 John Wiley & Sons, Inc.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 5
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 46 (1995), S. 514-524 
    ISSN: 0006-3592
    Keywords: glucose biosensor ; biosensor ; glucose oxidase ; cellulose binding domain (CBD) ; fermentation monitoring ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The design, construction, and characterization of a prototype-regenerable glucose biosensor based on the reversible immobilization of glucose oxidase (GOx) using cellulose binding domain (CBD) technology is described. GOx, chemically linked to CBD, is immobilized by binding to a cellulose matrix on the sensor-indicating electode. Enzyme immobilization can be reversed by perfusing the cellulose matrix with a suitable eluting solution. An autocavable sensor membrane system is employed which is shown to be practical for use in real microbial fermentations. The prototype glucose biosensor was used without failure or deterioration during fed-batch fermentations of Escherichia coli reaching a maximum cell density of 85 g (dry weight)/L. Medium glucose concentration based on sensor output correlated closely with off-line glucose analysis and was controlled manually at 0.44 ± 0.2 g/L for 2 h based on glucose sensor output. The sensor enzyme component could be eluted and replaced without interrupting the fermentation. To our knowledge, no other in situ biosensor has been used for such an extended period of time in such a high-cell-density fermentation. © 1995 John Wiley & Sons, Inc.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 6
    ISSN: 0006-3592
    Keywords: arg-gly-asp ; cellulose ; protein production ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The sequence Arg-Gly-Asp (RGD) in extracellular matrix proteins such as fibronectin, collagen, and laminin mediates cell attachment by interacting with proteins of the integrin family of cell surface receptors. A gene fusion encoding the RGD-containing peptide, fused to the C-terminus of a cellulose-binding domain (CBD/RGD), was expressed in Escherichia coli. Cultures produced up to 50 mg of CBD/RGD per liter, most of which was extracellular. It was purified from the culture supernatant by affinity chromatography on cellulose. CBD/RGD promoted the attachment of green monkey Vero cells to polystyrene and cellulose acetate. Attachment was inhibited by small synthetic peptides containing the RGD sequence. CBD/RGD was as effective as collagen in promoting the attachment of Vero cells to Cellsnow™ microcarriers. © 1995 John Wiley & Sons, Inc.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...