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  • Articles  (2)
  • Biology  (2)
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  • 1
    ISSN: 1420-9071
    Keywords: Complement ; pig ; complement ; system ; C3b receptor ; β-globulin ; macrophages
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The third component of the pig complement system (C3) was isolated in hemolytically active form and characterized. The C3 component is a β-globulin with the molecular weight of 191,000 and is composed of 2 non-identical polypeptide chains of Mt 112,000 and 74,000. The isolated C3 can be used for the detection of the C3b receptor on the membranes of heterologous peritoneal macrophages.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Antonie van Leeuwenhoek 52 (1986), S. 129-140 
    ISSN: 1572-9699
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Corynebacterium glutamicum CBII, in the stationary phase of growth, was found to produce spontaneously a substance resembling bacteriocins by its bactericidal properties. This substance designated glutamicin CBII was observed to exhibit bactericidal activity against coryneform bacteria (12 species tested) but not against unrelated gram-positive (3) and gram-negative (3) bacteria, while its action on bacteria with no quite known relatedness to the coryneform group (14) was found to be variable. Glutamicin CBII was partially purified by precipitation with ammonium sulphate (70% saturation), selective heat precipitation and gel chromatography on Sepadex G-50. The antibacterial substance diffused through cellophane membrane with an approximate cut-off of 10000 dalton and its sedimentation coefficient was determined to be 1.1. S by ultracentrifugation. Heating at 100°C for 30 min had no effect on its activity. Glutamicin CBII was proved to be resistant to chloroform, trypsin, chymotrypsin, pronase, and subtilisin. According to its staining behaviour and 1H NMR spectra it probably represents a glycoprotein containing only a minor protein component.
    Type of Medium: Electronic Resource
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