GLORIA

GEOMAR Library Ocean Research Information Access

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: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Synthesis of two recombinant proteins (human glucagon and human growth hormone) was investigated in fed-batch cultures at high cell concentrations of recombinant Escherichia coli. The glucose-limited growth was achieved without accumulation of metabolic by-products and hence the cellular environment is presumed invariable during growth and recombinant protein synthesis. Via exponential feeding in the two-phase fed-batch operation, the specific cell growth rate was successfully controlled at the desired rates and the fed-batch mode employed is considered appropriate for examining the correlation between the specific growth rate and the efficiency of recombinant product formation in the recombinant E. coli strains. The two recombinant proteins were expressed as fusion proteins and the concentration in the culture broth was increased to 15 g fusion growth hormone l−1 and 7 g fusion glucagon l−1. The fusion growth hormone was initially expressed as soluble protein but seemed to be gradually aggregated into inclusion bodies as the expression level increased, whereas the synthesized fusion glucagon existed as a cytoplasmic soluble protein during the whole induction period. The stressful conditions of cultivation employed (i.e. high-cell-density cultivation at low growth rate) may induce the increased production of various host-derived chaperones and thereby enhance the folding efficiency of synthesized heterologous proteins. The synthesis of the recombinant fusion proteins was strongly growth-dependent and more efficient at a higher specific growth rate. The mechanism linking specific growth rate with recombinant protein productivity is likely to be related to the change in cellular ribosomal content.
    Type of Medium: Electronic Resource
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Journal of industrial microbiology and biotechnology 22 (1999), S. 176-180 
    ISSN: 1476-5535
    Keywords: Keywords: Escherichia coli; mini-proinsulin; N-terminus residues; human tumor necrosis factor α; fusion partners
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Synthesis of human mini-proinsulin precursors was investigated in controlled fed-batch cultures at high cell concentrations of recombinant Escherichia coli. Transcription of the recombinant gene was controlled by a T7 promoter system. The human mini-proinsulin was prepared by substituting a C-chain peptide of natural proinsulin with a peptide sequence of only nine amino acids. The reduced size of fusion proinsulin and hence the increased purity of human insulin in the recombinant product may contribute to increasing the fermentation yield of human insulin. Three precursors (T1-, T2-, and T3-M2PI) were constructed by utilizing the N-terminus residues of human tumor necrosis factor α as fusion partners. The T2 precursor was most soluble in the cytoplasm, and exerted the most inhibitory effect on recombinant cell growth. In the production of T2-M2PI, significant amounts of undesirable metabolic by-products (acetate and ammonia) accumulated in the culture broth even at very low specific cell growth rate. The major portion of all synthesized precursors aggregated to insoluble inclusion bodies but the protein aggregates were easily converted to monomers in the presence of the anionic detergent (SDS) without using any reducing agent. With the expression of T1-M2PI, growth inhibition was minimal, and the maximum volumetric yield of mini-proinsulin (M2PI) in fermentation cultures was at the highest level among the synthesized precursors.
    Type of Medium: Electronic Resource
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
  • 3
    ISSN: 1573-2932
    Source: Springer Online Journal Archives 1860-2000
    Topics: Energy, Environment Protection, Nuclear Power Engineering
    Notes: Abstract SO2 concentrations have been measured for one year at forty-five locations throughout Asia using passive samplers. Duplicate samples were exposed at each site for one month intervals. The sites were selected to provide background information on the distribution of SO2 over wide geographical regions, with emphasis on the regional characteristics around areas estimated to be sensitive to sulfur deposition. The annual mean values ranged from less than 0.3 μg/m3 at Tana Rata, located at 1545 m on the Malaysia Peninsula, Lawa Mandau, (Borneo) Malaysia, and Dhankuta, Nepal, to values greater than 20 μg/m3 at Luchongguan (Guiyang) China, Babar Mahal, Nepal, and Hanoi, Vietnam. In general high concentrations were measured throughout China, with the highest concentrations in the heavy industrial areas in Guiyang. The concentrations in east Asia around the Korea peninsula were ∼5 μg/m3. The concentrations in the southeast Asia tropics were low, with no station in Malaysia and Indonesia having average concentrations exceeding 1.7 μg/m3. The observed SO2 concentrations were found to display a distinct seasonal cycle which is strongly influenced by the seasonality of winds and precipitation patterns.
    Type of Medium: Electronic Resource
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
  • 4
    Publication Date: 2013-01-04
    Description: Acanthamoeba myosin II (AMII) has two heavy chains ending in a 27-residue nonhelical tailpiece and two pairs of light chains. In a companion article, we show that five, and only five, serine residues can be phosphorylated both in vitro and in vivo: Ser639 in surface loop 2 of the motor...
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
  • 5
    Publication Date: 2012-05-10
    Description: A robust scanning diamond sensor for nanoscale imaging with single nitrogen-vacancy centres Nature Nanotechnology 7, 320 (2012). doi:10.1038/nnano.2012.50 Authors: P. Maletinsky, S. Hong, M. S. Grinolds, B. Hausmann, M. D. Lukin, R. L. Walsworth, M. Loncar & A. Yacoby
    Print ISSN: 1748-3387
    Electronic ISSN: 1748-3395
    Topics: Physics
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...