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  • 1
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Journal of agricultural and food chemistry 32 (1984), S. 379-382 
    ISSN: 1520-5118
    Source: ACS Legacy Archives
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Journal of agricultural and food chemistry 38 (1990), S. 743-747 
    ISSN: 1520-5118
    Source: ACS Legacy Archives
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
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  • 3
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Journal of agricultural and food chemistry 37 (1989), S. 119-122 
    ISSN: 1520-5118
    Source: ACS Legacy Archives
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Experiments in fluids 12 (1991), S. 41-48 
    ISSN: 1432-1114
    Source: Springer Online Journal Archives 1860-2000
    Topics: Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
    Notes: Abstract It is well documented that a trailing vortex pair approaching the ground, and a vortex ring colliding head-on with a rigid plane, experience a reversal in axial velocity which is commonly referred to as “rebound”. One explanation of this phenomenon suggests that it is essentially an inviscid process due to the effect of the finite core-size, whereas another and more widely accepted explanation attributes it to the influence of a secondary vortex which is generated at the surface by viscous effects. The aim of this paper is to assess experimentally the validity of these competing explanations. To achieve this, flow visualization studies of the collision of a vortex ring with a wall are compared with those of the head-on collision of two identical rings. The head-on collision is designed to mimic the inviscid, free-slip case of a ring/wall interaction. This paper describes the experimental findings.
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    European journal of clinical pharmacology 40 (1991), S. 603-607 
    ISSN: 1432-1041
    Keywords: Gallopamil ; protein binding ; albumin ; α1-acid glycoprotein ; interspecies differences
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Medicine
    Notes: Summary There is little information about the factors which influence drug protein binding between species. We have therefore investigatived the role of pH on the binding of gallopamil, a calcium channel antagonist known to exhibit pH-sensitive binding, among four species, human, baboon, bovine, and canine. We used pure protein solutions of α1 acid glycoprotein (AAG) (60 mg·l−1), albumin (45 gm·l−1), and their combination and three values of pH, 7.0, 7.4, and 8.0. Gallopamil protein binding was determined over a concentration range of 2.0×10−7mol·l−1 to 2.1×10−3mol·l−1 using equilibrium dialysis. Gallopamil binding in all solutions was best described using a two binding site model in the combination solution and a one binding site model in the pure solutions. pH did not affect the number of identical binding sites. However, the influence of pH on gallopamil binding was species specific. Increasing the pH from 7.0 to 8.0 influenced binding affinity differently between species. There were directionally similar changes in unbound fraction at a gallopamil concentration of 2×10−7mol·l−1 as pH increased, although there were species differences in the degree of change. In protein solutions containing both AAG and albumin a reduction in pH from 7.4 to 7.0 resulted in species-specific increases in the unbound fraction. Increasing the pH from 7.4 to 8.0 again resulted in species-specific reductions in the unbound fraction of gallopamil. Similar changes were seen when pure AAG or albumin solutions were used, indicating species variance in both gallopamil protein binding and the effect of pH on binding.
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  • 6
    Electronic Resource
    Electronic Resource
    Bradford : Emerald
    Accounting, auditing & accountability journal 10 (1997), S. 175-197 
    ISSN: 0951-3574
    Source: Emerald Fulltext Archive Database 1994-2005
    Topics: Economics
    Notes: Examines the three-way interaction between budget emphasis, participation and task difficulty affecting managerial performance within the framework suggested by Harrison (1992) with a sample of 197 functional heads from Singaporean and Australian manufacturing companies. The results support a three-way interaction between budget emphasis, budgetary participation and task difficulty affecting managerial performance and second, cultural differences between Singapore and Australia (pertaining to power distance) which interact neither with budgetary participation nor budget emphasis. The results also suggest that high budgetary participation (regardless of budget emphasis) in high task difficulty situations and high budget emphasis (regardless of budgetary participation) in low task difficulty situations are associated with improved managerial performance in Singapore and Australia.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 46 (1981), S. 0 
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Textural modification of fish protein gels by incorporation of plastic fat was investigated by examining the effect of the physical properties of fat on the structure and the material properties of protein gels. Material properties of fat-containing protein gels were influenced largely by fat distribution pattern which was, in turn, affected by fat hardness. Both compressive and shear forces reached their maximum when fat of 1.8 cm–1 hardness index (HI) was added at a level of 15% (fat/muscle). Addition of medium hard fat (0.54–0.78 cm–1 HI): (1) prevented a sponge-like texture development by improving freeze-thaw stability; (2) increased plastic deformation, thus making cooked gels less rubbery; (3) overcame the weakening of texture caused by cooking at the critical zone (60–70°C); and, (4) minimized the variations in textural strength resulting from cooking.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 41 (1976), S. 0 
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Factors affecting textural characteristics of cooked comminuted fish muscle were investigated. These factors included: time of comminution, presence of NaCl or NaCl and polyphosphates, effect of mechanical deboning, temperature of cooking, and type of heating medium used. Textural characteristics were evaluated objectively using as an index: compressive strength, modulus of elasticity, resilience, and shear strength. The change in the physical state of the protein-water system was determined from the quantity of fluid (expressible fluid) that can be expressed from the specimen subjected to a fixed compression force. With extensive chopping, mechanical strength diminished as the concentration of extractable myosin in the muscle homogenates decreased. Changes in expressible fluid followed changes in physical properties. Formulations with higher moisture contents were more susceptible to adverse changes brought about by mechanical treatments such as chopping. Mechanical strength of the cooked comminuted muscle progressed in the order of increasing strength as follows: no additives, with NaCl, with NaCl and polyphosphates. The presence of polyphosphates allowed increased solubilization of muscle protein and improved water binding. The variation in textural strength of products receiving different preheating treatments appeared to be related to the changes in water binding as shown by the inverse relationship of mechanical strength to the quantity expressible fluid. The textural strength of cooked muscle homogenates decreased in the order of: steamed, water cooked, and smoke-house cooked.
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  • 9
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Biochemical and Biophysical Research Communications 139 (1986), S. 455-460 
    ISSN: 0006-291X
    Keywords: [abr] Protein I; the oligomeric form of p36 (36"210"2) ; [abr] p36; Protein I, Phospholipase A"2, lipocortin
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Biochemical and Biophysical Research Communications 139 (1986), S. 455-460 
    ISSN: 0006-291X
    Keywords: [abr] Protein I; the oligomeric form of p36 (36"210"2) ; [abr] p36; Protein I, Phospholipase A"2, lipocortin
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
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