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  • Articles  (55)
  • monoclonal antibody  (47)
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  • Springer  (55)
  • Process Engineering, Biotechnology, Nutrition Technology  (55)
  • 1
    Electronic Resource
    Electronic Resource
    Production of monoclonal antibodies and ELISA for thebaine and codeine (1995)
    Springer
    Cytotechnology 19 (1995), S. 55-61 
    Details
    ISSN: 1573-0778
    Keywords: codeine ; ELISA ; monoclonal antibody ; opium alkaloid ; qualitative analysis ; thebaine
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract The ratio of hapten and bovine serum albumin in antigen conjugate was exactly determined by matrix-assisted laser desorption/ionization mass spectrometry. Monoclonal antibodies against thebaine and codeine were produced by hybridoma fused with the sprenocytes immunized with thebaine- and codeine-bovine serum albumin conjugate and HAT-sensitive mouse myeloma cell line, P3-X63-Ag8-653. No cross-reaction of anti-thebaine antibody against morphine was observed. Very small cross-reaction appeared in codeine (0.004%). The cross-reaction of anti-codeine antibody against morphine and thebaine was 2.97 and 5.98%, respectively. The full measuring range of the assay extends from 60 pg mL to 1 ng mL for thebaine and 1 ng mL to 100 ng mL for codeine.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00749755
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  • 2
    Electronic Resource
    Electronic Resource
    High density culture of mouse-human hybridoma cells using a perfusion culture apparatus with multi-settling zones to separate cells from the culture medium (1989)
    Springer
    Cytotechnology 2 (1989), S. 5-8 
    Details
    ISSN: 1573-0778
    Keywords: hybridoma ; monoclonal antibody ; perfusion culture ; mammalian cell culture ; serum-free culture
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Mouse-human hybridoma X87X cells were cultivated using a novel perfusion culture apparatus provided with three-settling zones to separate the cells from the culture medium by gravitational settling. The maximum viable cell density in a serum-free culture medium attained 3.0×107 cells/ml, when the specific perfusion rate was set to 2.3 vol day-1, and monoclonal antibody was continuously produced. These results were almost the same as those in the perfusion culture vessel with one settling zone and revealed that the process with a plurality of settling zones is a promising one for scale-up of a gravitation type of perfusion culture vessel.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00365409
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  • 3
    Electronic Resource
    Electronic Resource
    SSGF-I, a potent growth-promoting substance for mammalian cells from swine serum (1989)
    Springer
    Cytotechnology 2 (1989), S. 9-17 
    Details
    ISSN: 1573-0778
    Keywords: heterohybridoma ; LDL ; monoclonal antibody ; serum-free medium ; PEG ; swine serum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract A small amount of swine serum markedly stimulated cell growth for high productivity subclones derived from a mouse human-human heterohybridoma, N12-16.63, secreting an anti-tetanus toxoid human monoclonal antibody in a polyethylene glycol (PEG)-containing serum-free medium, PEG-86-1. A growth promoting substance, SSGF-I, was isolated from the serum by ammonium sulfate fractionation, Cibacron blue F3A-G affinity chromatography, DEAE-agarose ion exchange chromatography, and gel filtrations on Trisacryl GF 2000 and Sephacryl S-300. SSGF-I was characterized as a low density lipoprotein (LDL) of swine serum by its physico-chemical properties. It promoted cell growth synergistically with PEG and its optimum concentration was 1 to 100μg/ml. Human LDL was less active, and human or swine high density lipoprotein (HDL) and very low density lipoprotein (VLDL) were inactive. Based on these results, we propose an improved serum-free medium, PEG-86-3, which contains all the ingredients of PEG-86-1 and 10μg/ml SSGF-I. This medium is useful for not only high productivity heterohybridomas but also for a variety of lymphoid cell lines.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00365410
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  • 4
    Electronic Resource
    Electronic Resource
    A serum-free medium for hybridoma cell culture (1993)
    Springer
    Cytotechnology 11 (1993), S. 169-174 
    Details
    ISSN: 1573-0778
    Keywords: cell culture ; hybridoma ; monoclonal antibody ; serum-free medium
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract The effects of several different substances, including insulin, transferrin, ethanolamine, selenite and butyrate on the growth of murine hybridoma 2F7 cells, which secrete monoclonal antibody against small cell lung cancer, were investigated, and a serum-free medium SFMI was formulated. The effects of taurine, spermidine, progesterone and adenine on the cell growth were tested further on the basis of the medium SFMI, and a modified serum-free medium SFM II was established. On the basis of medium SFM II, the substitution tests of ferric citrate for transferrin were carried out, and it was found that transferrin could be replaced. The experiments suggested that the formulated serum-free medium was suitable for 2F7 cell growth and monoclonal antibody secretion, and thus facilitated subsequent purification of monoclonal antibody.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00749866
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  • 5
    Electronic Resource
    Electronic Resource
    Rapid separation of solasodine glycosides by an immunoaffinity column using anti-solamargine monoclonal antibody (1999)
    Springer
    Cytotechnology 31 (1999), S. 153-158 
    Details
    ISSN: 1573-0778
    Keywords: immunoaffinity column ; MALDI-MS ; monoclonal antibody ; solasodine glycosides
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Immunoaffinity column using anti-solamargine monoclonal antibody for separation of solasodine glycosides was established. This method was specific for solasodine glycosides which was detected by thin layer chromatography and the western blotting. Total solasodine glycosides have been separated directly from the crude extract of Solanum khasianum fruit by the newly established immunoaffinity column.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1008032524419
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  • 6
    Electronic Resource
    Electronic Resource
    Electron microscopy of hybridoma cells with special regard to monoclonal antibody production (1990)
    Springer
    Cytotechnology 4 (1990), S. 13-28 
    Details
    ISSN: 1573-0778
    Keywords: monoclonal antibody ; hybridoma ; electron microscopy ; endoplasmic reticulum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Electron microscopy of mouse hybridoma cell lines shows that the major difference between non, low and high producer cell lines is the amount of endoplasmic reticulum. Vesicular-tubular or cavernous structures of endoplasmic reticulum, which can survive long after cell death, are particularly abundant in producer cell lines. Immunogold labelling with anti-mouse IgG reveals that antibodies are predominantly located in these structures. The cell membrane undergoes structural changes during the late stages of batch culture with the disappearance of microvilli and the appearance of blebs and deep indentations. Necrosis disrupts the cytoplasmic structures and the nucleus is last to degrade.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00148807
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  • 7
    Electronic Resource
    Electronic Resource
    Antibody production in packed bed reactors using serum-free and protein-free medium (1990)
    Springer
    Cytotechnology 4 (1990), S. 279-283 
    Details
    ISSN: 1573-0778
    Keywords: animal cell culture ; hybridoma ; monoclonal antibody ; packed bed reactor ; continuous culture ; perfusion ; protein-free medium
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract The present work demonstrates the utility of packed bed reactors for the production of monoclonal antibody. We present data from a continuous process run for the production of over 100 grams of antibody, using serum-free medium. An additional pilot run also demonstrates the potential for continued antibody production under protein-free conditions, using a standard basal medium.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00563788
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  • 8
    Electronic Resource
    Electronic Resource
    Cell cycle kinetics of the accumulation of heavy and light chain immunoglobulin proteins in a mouse hybridoma cell line (1994)
    Springer
    Cytotechnology 14 (1994), S. 205-218 
    Details
    ISSN: 1573-0778
    Keywords: Cell cycle ; flow cytometry ; heavy chain ; hybridoma ; light chain ; monoclonal antibody ; population balance
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Rates of accumulation of immunoglobulin proteins have been determined using flow cytometry and population balance equations for exponentially growing murine hybridoma cells in the individual G1, S and G2+M cell cycle phases. A producer cell line that secretes monoclonal antibodies, and a nonproducer clone that synthesizes only κ-light chains were analyzed. The pattern for the kinetics of total intracellular antibody accumulation during the cell cycle is very similar to the previously described pattern for total protein accumulation (Kromenaker & Srienc 1991). The relative mean rate of heavy chain accumulation during the S phase was approximately half the relative mean rate of light chain accumulation during this cell cycle phase. This indicates an unbalanced synthesis of heavy and light chains that becomes most pronounced during this cell cycle phase. The nonproducer cells have on average an intracellular light chain content that is 42% lower than that of the producer cells. The nonproducer cells in the G1 phase with low light chain content did not have a significantly higher rate of light chain accumulation relative to other G1 phase nonproducer cells. This is in sharp contrast to what was observed for the G1 phase producer cells. In addition, although the relative mean rate of accumulation of light chain was negative for G2+M phase nonproducer cells, the magnitude of this relative mean rate was less than half that observed for the producer cells in this cell cycle phase. This suggests that the mechanisms that regulate the transport of fully assembled antibody molecules through the secretion pathway differ from those which regulate the secretion of free light chains. The results reported here indicate that there is a distinct pattern for the cell cycle dynamics of antibody synthesis and secretion in hybridomas. These results are consistent with a model for the dynamics of secretion which suggests that the rate of accumulation of secreted proteins will be greatest for newborn cells due to an interruption of the secretion pathway during mitosis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00749617
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  • 9
    Electronic Resource
    Electronic Resource
    Methods and strategies available for the process control and optimization of monoclonal antibody production (1994)
    Springer
    Cytotechnology 14 (1994), S. 219-232 
    Details
    ISSN: 1573-0778
    Keywords: animal cells ; cellular metabolism ; cultivation ; hybridomas ; modelling ; monoclonal antibody ; process control ; optimisation ; simulation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract The objective of this paper is to explore the range of methods and strategies available for the process control and optimization of monoclonal antibody production by hybridoma cell culture. Emphasis will be placed on the choice of the level of complexity incorporated into the process control and optimisation procedure. It will be shown that the behaviour of hybridomas in culture is influenced by sophisticated cellular metabolic activities and various interactive environmental factors and that the understanding and modelling of the way hybridomas grow in the bioreactor should enable optimisation of bioreactor operating conditions to achieve maximum monoclonal antibody formation. However, due to the lack of on-line instrumentation of important biological variables and the incomplete knowledge of hybridoma cultivation process, there exist many limitations and challenges to the advent of applications of process control and optimisation in this field. To solve the problem, introduction of industrially practical biological measurements and development of new control concepts are inevitable. At the end of this paper, we shall discuss possible schemes for the control of the physsiological state of cells in order that balanced cell growth and maximum monoclonal antibody synthesis may be achieved.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00749618
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  • 10
    Electronic Resource
    Electronic Resource
    Weaning of three hybridoma cell lines to serum free low protein medium (1991)
    Springer
    Cytotechnology 6 (1991), S. 65-78 
    Details
    ISSN: 1573-0778
    Keywords: hybridoma ; monoclonal antibody ; serum free culture ; low protein medium ; weaning protocol
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract A general weaning procedure is described which allowed a range of hybridomas to be weaned readily off serum without loss of antibody production. Initial work was carried out with one cell line only (SPO1 cells) and one serum substitute containing a final protein concentration of 40 mg l-1. The SPO1 cells were first adapted to a range of readily available basal media and then weaned off serum by a range of protocols. From this work an optimal weaning protocol and basal medium for weaning were determined. These were then used to wean the SPO1 cells and two other cell lines off serum with a second, protein free, serum substitute with varying concentrations of defined proteins added. All three cell lines investigated were readily weaned off serum by this protocol at protein concentrations as low as 1 mg l-1. No loss of antibody production was observed with any of the cell lines. The weaning procedure outlined is both simple and rapid and has been successfully adopted in our laboratory by relatively inexperienced cell culture technicians.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00353704
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