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  • 1
    Electronic Resource
    Electronic Resource
    Chemical and ultrastructural investigations of Mycobacterium bovis BCG: implications for the molecular structure of the mycobacterial cell envelope (1996)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS immunology and medical microbiology 15 (1996), S. 0 
    Details
    ISSN: 1574-695X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Abstract The mycobacterial cell wall visualized by transmission electron microscopy (TEM) of thin sections of resin-embedded specimens is generally believed to consist of an electron-dense peptidoglycan, an electron-transparent arabinogalactan-mycolate layer and an electron-dense outer layer (OL). In addition, a pseudocapsule known as the ‘electron-transparent zone’ (ETZ) has been observed after phagocytosis of mycobacteria by macrophages. TEM of thin sections of Mycobacterium bovis BCG, Tice® substrain, revealed an OL bilayer, each of which measured 2–4 nm in diameter. The intermediate electron-transparent layer varied from 1 to about 250 nm in diameter and appears to be a previously observed oxygen-dependent amorphous integument that consists of hot water-extractable neutral polysaccharides, especially a recently characterized α-glucan, comprising about 12% of the dry cell weight. This and other recent studies of BCG have revealed cell-surface features that may provide a better understanding of the outer mycobacterial cell envelope.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-695X.1996.tb00087.x
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  • 2
    Electronic Resource
    Electronic Resource
    Preparation of Small Gelatin and Albumin Microparticles by a Carbon Dioxide Atomization Process (1993)
    Springer
    Pharmaceutical research 10 (1993), S. 1385-1388 
    Details
    ISSN: 1573-904X
    Keywords: gelatin microparticles ; albumin microparticles ; carbon dioxide atomization ; Turbotak
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1018946503069
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  • 3
    Electronic Resource
    Electronic Resource
    Optimization of Conditions for Preparing 2- to 5-Micron-Range Gelatin Microparticles by Using Chilled Dehydration Agents (1993)
    Springer
    Pharmaceutical research 10 (1993), S. 621-626 
    Details
    ISSN: 1573-904X
    Keywords: gelatin microparticles ; chilled dehydration process ; factorial design ; process optimization
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1018974708637
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  • 4
    Electronic Resource
    Electronic Resource
    The Influence of Free Fatty Acid Formation on the pH of Phospholipid-Stabilized Triglyceride Emulsions (1993)
    Springer
    Pharmaceutical research 10 (1993), S. 774-776 
    Details
    ISSN: 1573-904X
    Keywords: phospholipids ; thermal degradation ; triglyceride emulsions ; pH ; free fatty acids
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1018932421357
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  • 5
    Electronic Resource
    Electronic Resource
    The Effect of Compactional Pressure on Urease Activity (1988)
    Springer
    Pharmaceutical research 5 (1988), S. 776-780 
    Details
    ISSN: 1573-904X
    Keywords: urease activity ; dry-state compaction ; protein drugs
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Jack bean urease is a proteinaceous enzyme, MW approximately 489 kD, readily soluble in water but losing activity when sheared in solution at stresses as low as 2.5 Pa. There is a need for controlled-release forms of many of the new genetically engineered peptide and polypeptide drugs with high specific activities. The simplest form of controlled release would be a sterile compressed pellet of the active component inserted subdermally. However, “activity” may be lost on compaction. Urease can be regarded as a model protein which may lose activity when sheared during compaction in the dry state. Tablets of urease weighing 100 mg were compressed over a range of pressures from 60 to 1750 MPa. No relative loss of activity would be detected following compaction at pressures up to 474 MPa. Above this limiting pressure there was a 50% loss of relative activity, evidently by a compactional effect on the protein quaternary and tertiary structures. No direct relationship was observed between stress (compactional pressure) and inactivation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1015988718381
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  • 6
    Electronic Resource
    Electronic Resource
    A scanning electron microscope study of mycobacterial developmental stages in commercial BCG vaccines (1991)
    Springer
    Current microbiology 22 (1991), S. 247-252 
    Details
    ISSN: 1432-0991
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Scanning electron microscopy (SEM) studies were performed on freshly prepared and freeze-dried Tice™-substrainMycobacterium bovis BCG vaccine as well as Tice BCG grown on Middlebrook 7H10 agar. Intact colonies of the Tice and Glaxo BCG substrains growing on agar were also examined. The presence of developmental stages of the mycobacterial life cycle previously reported in the literature was confirmed in actively growing BCG and in commercial vaccine preparations. The pleomorphic forms consisted of various size coccal and bacillary cells. Propagation appeared to occur by fission of both forms to produce aggregate bodies and by a coccal-bacillary cycle. Filterable (30–200 nm) granular cocci and coccal microcolonies were also observed in commercially prepared BCG vaccines. The implications of pleomorphism on the biologic activities of various BCG vaccines are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02092317
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  • 7
    Electronic Resource
    Electronic Resource
    Size Characterization of Mycobacterium bovis BCG (Bacillus Calmette Guérin) Vaccine, Tice™ Substrain (1988)
    Springer
    Pharmaceutical research 5 (1988), S. 607-610 
    Details
    ISSN: 1573-904X
    Keywords: Bacillus Calmette Guérin (BCG), Tice™ ; HIAC/Royco ; Coulter ; size analysis ; aggregation number ; colony-forming units (CPU) ; aggregation mechanism ; surface charge ; Mycobacterium bovis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Reconstituted, lyophilized, attenuated Mycobacterium bovis, Bacillus Calmette Guérin (BCG) vaccine, Tice™ substrain, was characterized using a Coulter Multisizer and a HIAC/Royco counter. The primary organism has an equivalent spherical diameter approximating 1 µm but the BCG cell suspension is heavily aggregated. The cumulative size distribution of the suspension fits a log-probit plot and this information can be used to determine the total number of particles per ampoule. The instrumental count may be related to the viable count. The state of dispersion was unaffected by mild shear (syringe aspiration or ultrasound) and only slightly affected by the addition of cetylpyridinium chloride or sodium tauroglycolate.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1015954316139
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  • 8
    Electronic Resource
    Electronic Resource
    The Effect of Compactional Pressure on a Wheat Germ Lipase Preparation (1990)
    Springer
    Pharmaceutical research 7 (1990), S. 247-250 
    Details
    ISSN: 1573-904X
    Keywords: lipase ; compaction ; activity loss
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Wheat germ lipase is a relatively homogeneous proteinaceous enzyme known to suffer inactivation by compactional pressure. However, earlier investigators suggested that the inactivation was due to thermal degradation following the application of mechanical energy. A wheat germ preparation (Sigma) was compacted over a range of pressures from 85 to 1800 MPa. The 100-mg compacts were carefully dispersed and dissolved in aqueous 0.05 M potassium phosphate buffer, pH 7.4, and the biological activity was determined using triacetin as a substrate. No significant loss of activity occurred up to a pressure of 175 MPa. After this point, a discontinuity was evident with a loss of 30% activity but this loss of activity remained constant over the remainder of the applied pressure range studied. The density/applied pressure relationship indicated that the discontinuity was due to space constraints. The density failed to go higher than a limiting value of approximately 1.2 g cm−3, irrespective of the applied pressure. There was an approximately linear relationship between the relative loss of biological activity and density, indicating that the observed loss of biological activity is unlikely to be due to applied thermal energy but more likely to be due to space constraints on the volume occupied by the molecule. However, circular dichroism measurements and SDS-PAGE examination did not reveal any obvious protein structural changes, suggesting that the mechanism involved in activity loss is subtle.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1015817927505
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  • 9
    Electronic Resource
    Electronic Resource
    Water Vapor Adsorption and Desorption Isotherms of Biologically Active Proteins (1991)
    Springer
    Pharmaceutical research 8 (1991), S. 191-195 
    Details
    ISSN: 1573-904X
    Keywords: urease ; lipase ; α-amylase ; β-glucuronidase ; isolated soy protein ; static/dynamic water adsorption and desorption
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Using a protein isolated from soy, a dynamic water adsorption method was developed and the data were compared with those obtained from a static gravimetric procedure. Both methods gave comparable results, showing that Type II isotherms with considerable hysteresis were obtained. However, the dynamic procedure was preferred since it provided data rapidly and used significantly less material. Using the dynamic method, water adsorption isotherms at 25°C were also determined for four biologically active proteins: α-amylase, (β-glucuronidase, lipase, and urease. BET (Brunauer, Emmet, and Teller) parameters were calculated and the specific surface areas for the native, biologically active proteins were found to be similar, 238.4 ± 20.2 m2/g. On the other hand, the specific surface area for the denatured soy protein isolate was 144.6 m2/g. Nevertheless, the heat of absorbance for all of the proteins examined was similar, suggesting that they have comparable degrees of hydrophilicity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1015835902721
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  • 10
    Electronic Resource
    Electronic Resource
    Production of 5–15 µm Diameter Alginate-Polylysine Microcapsules by an Air-Atomization Technique (1991)
    Springer
    Pharmaceutical research 8 (1991), S. 341-344 
    Details
    ISSN: 1573-904X
    Keywords: alginate/polylysine microcapsules ; atomization technique ; 5–15 µm microcapsules ; Bacillus Calmette Guérin (BCG) vaccine
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract A novel method of preparing small-sized microcapsules using a Turbotak air-atomizer is reported. Alginate-polylysine microcapsules containing Bacillus Calmette Guérin vaccine have been prepared by an adaptation of the method of Lim (1) which allows the manufacture of small-sized microcapsules. A Turbotak is used to spray sodium alginate solution into calcium chloride solution to form temporary calcium alginate microgel capsules. These temporary microgel droplets are subsequently cross-linked with polylysine to form permanent membranes. Microcapules in the size range of 5–15 µm have been produced which can be compared to an average diameter of ≥300 µm obtained by the method reported by Lim. The microcapsule size is dependent on the conditions of operation of the Turbotak and the concentration of the sodium alginate solution. Particles within the size range 5–15 µm can be reproducibly manufactured using the conditions of operation reported here. Other size ranges below the minimum of 300 µm reported by Lim are also feasible using this technique.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1015841531372
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