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  • 1995-1999  (2)
  • Keywords: baculovirus–insect cell expression vector system (BEVS); Sf-9; HSV protease; glutathione-S-transferase  (1)
  • Chemistry
  • Ultrasound technique
Source
Material
Years
Year
Keywords
  • 1
    Electronic Resource
    Electronic Resource
    Technique of laparoscopic ultrasound examination of the liver and pancreas (1996)
    Springer
    Surgical endoscopy and other interventional techniques 10 (1996), S. 684-689 
    Details
    ISSN: 1432-2218
    Keywords: Laparoscopic ultrasound ; Intraoperative ultrasound ; Ultrasound technique ; Liver ; Pancreas
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Since the introduction of a recent laparoscopic ultrasound (LU), the value of this modality in examining the liver and pancreas has been reported. However, a precise scanning technique of LU has not previously been described. Based on our experience with intraoperative ultrasound during laparotomy, we have developed a technique for complete examination of the entire organs using a rigid LU probe. A 7.5-MHz rigid probe, 10 mm in diameter, was employed. The scanning was performed through three trocar ports: right subcostal, subxiphoid, and umbilical. For the liver, the subcostal scanning provided fundamental transverse views. The subxiphoid and umbilical scanning delineated the areas unable to be imaged by the subcostal scanning. For the pancreas, the subcostal and umbilical scanning demonstrated longitudinal and transverse views, respectively. The subxiphoid scanning enhanced examination of the pancreatic head. Three basic probe maneuvers (advancement-withdrawal, lateral movement, and rotation) and various scanning techniques (contact, probe-standoff, and compression scanning) should be utilized appropriately. With a rigid probe, complete LU examination of the liver and pancreas is possible using these techniques. We believe the present scanning method will help more surgeons learn LU.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00188531
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Production of recombinant herpes simplex virus protease in 10-L stirred vessels using a baculovirus–insect cell expression system (1997)
    Springer
    Journal of industrial microbiology and biotechnology 19 (1997), S. 87-91 
    Details
    ISSN: 1476-5535
    Keywords: Keywords: baculovirus–insect cell expression vector system (BEVS); Sf-9; HSV protease; glutathione-S-transferase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: A gene expression system using recombinant Autographa californica nuclear polyhedrosis virus (baculovirus) and Sf-9 cells has been scaled up to the 10-L tank level and shown to be capable of producing herpes simplex virus (HSV) protease in serum-free media. High densities of Spodoptera frugiperda (Sf-9) cells were achieved by modifying two 10-L Biolafitte fermenters specifically for insect cell growth. The existing Rushton impellers were replaced by marine impellers to reduce shear and the aeration system was modified to allow external addition of air/O2 mixtures at low flow rates through either the sparge line or into the head space of the fermenter. To inoculate the tanks, Sf-9 cells were adapted to grow to high cell densities (6–10 × 106 cells ml−1) in shake flasks in serum-free media. With these procedures, cell densities of 5 × 106 cells ml−1 were routinely achieved in the 10-L tanks. These cells were readily infected with recombinant baculovirus expressing the 247-amino acid catalytic domain of the HSV-1 strain 17 protease UL26 gene as a glutathione-S-transferase (GST) fusion protein (GST-247). Three days after infection at a multiplicity of infection (MOI) of 3 pfu cell−1, the GST-247 fusion protein was purified from a cytoplasmic lysate by Glutathione Sepharose 4-B affinity chromatography with reproducible yields of 11–38 mg L−1 of recombinant protein and ≥ 90% purity. Maximum production of this protein was observed at a cell density of 5.0 × 106 cells ml−1.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/sj.jim.2900446
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    Paper (German National Licenses)
    Fulltext
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