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  • 1
    Electronic Resource
    Electronic Resource
    Epidural anaesthesia in the presence of a cerebral tumour (1987)
    Oxford, UK : Blackwell Publishing Ltd
    Anaesthesia 42 (1987), S. 0 
    Details
    ISSN: 1365-2044
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2044.1987.tb04002.x
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    The effect of normobaric hyperoxia on cardiac index in healthy awake volunteers (2003)
    Oxford, UK : Blackwell Science Ltd
    Anaesthesia 58 (2003), S. 0 
    Details
    ISSN: 1365-2044
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Fifteen healthy volunteers were exposed to a stepwise increase in FIO2 between 0.21 and 1.0, and their haemodynamic responses were measured with a non-invasive transthoracic bio-impedance monitor. There was mean reduction in cardiac index from 3.44 to 3.08 l.min−1.m−2 (10.7%, p 〈 0.001). The mean reduction in heart rate was from 77.3 to 69.1 beats.min−1 (10.5%, p 〈 0.001) and the mean systemic vascular index increased from 2062 to 2221 dyne.s−1.cm−5.m−2 (7.7%, p 〈 0.025). There were no significant changes in stroke index or mean arterial pressure. These changes are similar quantitatively and qualitatively to those previously reported by dye dilution techniques.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2044.2003.03333.x
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  • 3
    Electronic Resource
    Electronic Resource
    FUNCTIONAL PROPERTIES OF NOVEL PROTEINS: ALFALFA LEAF PROTEIN (1976)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 41 (1976), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Functional properties of protein concentrates from alfalfa leaves (ALP) prepared by several methods were determined. Minimum solubilities occurred around pH 3.5–4; sodium chloride 0.05–0.2M had little effect on minimum solubility. Extraction of the lipids from ALP with acetone decreased solubility slightly; increased the bulk density (2-3-fold); and reduced water and fat absorption capacities by 50% compared to the controls. Both emulsifying activities and emulsion stabilities of ALP samples were generally better than those of soy protein concentrate but poorer than those of soy sodium proteinate i.e., average of 57, 48 and 87 and 60, 50 and 90%, respectively. Emulsifying capacity of ALP samples were reduced following acetone extraction.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1976.tb00602.x
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  • 4
    Electronic Resource
    Electronic Resource
    COMPOSITION OF ALFALFA LEAF PROTEIN ISOLATES (1975)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 40 (1975), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1975.tb01041.x
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  • 5
    Electronic Resource
    Electronic Resource
    PROTEIN PRODUCTION FROM CRUDE LACTOSE BY Saccharomyces fragilis. (1975)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 40 (1975), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1975.tb00566.x
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  • 6
    Electronic Resource
    Electronic Resource
    COMPOSITION OF THE MYCELIUM OF Penicillium roqueforti (1977)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 42 (1977), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The proximate chemical and detailed lipid composition of the vegetative mycelium of the mold Penicillium roqueforti were determined. Maximum lipid accumulation in the mycelium of P. roqueforti occurred at a growth temperature of 25°C, and a culture age of 120 hr when mold cultures were grown in liquid submerged corn steep liquor/sucrose media. The dry mycelium consisted of 48.3, 37.8, 10.4 and 3.5% of carbohydrate, crude protein (N × 6.25), lipid and ash, respectively. The amino acid composition of the protein from P. roqueforti was excellent, being only slightly deficient in methionine. The levels of leucine, aspartic and glutamic acid residues were high. Neutral lipids were composed of triglycerides, 33.8%; diglycerides, 1.7%; free fatty acids, 8.1%; and nonsaponifiable material, 8.1% of the total lipids, respectively. Phospholipids comprised 35.3% and glycolipids 7.4% of the total lipids. Palmitic, stearic, oleic, and linoleic acids were the major fatty acid components of the total lipids of P. roqueforti mycelia.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1977.tb12578.x
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  • 7
    Electronic Resource
    Electronic Resource
    FUNCTIONAL PROPERTIES OF ALFALFA LEAF PROTEIN: FOAMING (1976)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 41 (1976), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Alfalfa leaf proteins extracted with sodium chloride (1M), sodium hydroxide (0.05M) or Tris buffer (0.1M) had poor foaming properties compared to proteins obtained by direct expression of leaf juice. Extraction of lipids from all protein extracts markedly improved both foam formation and foam stability. Foam expansion of alfalfa leaf protein surpassed that of ovalbumin but the foam was less stable. The pH foam expansion profile resembled the solubility pattern of this protein. The delipidated protein preparations showed little pH effect being rather constant between pH 2–10. Foam stability of all preparations was markedly pH dependent showing minima in the isoelectric range around pH 3.5. Both sucrose and sodium chloride reduced the foaming of leaf proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1976.tb00655.x
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  • 8
    Electronic Resource
    Electronic Resource
    Amylase Activity in Banana Fruit: Properties and Changes in Activity with Ripening (1981)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 46 (1981), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Following subcellular fractionation and centrifugation, the amylase activity was located in the cytosol fraction of banana fruit. Over 80% of the observed activity (15—20 units per mg of protein) was attributed to α-amylase. The activity of β-amylase was tenfold lower and starch phosphorylase activity was low (17 μg inorganic phosphorus released per mg protein per 24 hr.). The activity of amylase in crude preparations was stimulated 40% by calcium ions. The amylase preparation, which was very stable at 4°C, hydrolyzed soluble potato starch and banana starch at similar rates. Maximum activity was observed between pH 6—7. The energy of activation of hydrolysis was 9.74 Kcal/mole. Amylase was quite active up to 62°C but rapidly lost activity above this temperature. There was an approximate twofold increase in amylase during the initial phase of ripening.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1981.tb04183.x
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  • 9
    Electronic Resource
    Electronic Resource
    EFFECTS OF MICROWAVE COOKING ON FOOD FATTY ACIDS: NO EVIDENCE OF CHEMICAL ALTERATION OR ISOMERIZATION (1980)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 45 (1980), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Because of the current interest in the potential physiological effects of trans fatty acids and a brief report that microwave cooking causes isomerization of unsaturated fatty acids, we examined the effects of microwave treatments on the fatty acid composition of several food lipids, i.e., chicken fat, beef tallow, bacon fat, rainbow trout, peanut oil, and potato lipids. The data indicate that microwave cooking per se does not change the fatty acid pattern of these lipids nor cause isomerization of the unsaturated fatty acids.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1980.tb07604.x
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  • 10
    Electronic Resource
    Electronic Resource
    ANTIOXIDANT EFFECTS OF SOY PROTEIN HYDROLYSATES ON COPPER-CATALYZED METHYL LINOLEATE OXIDATION (1980)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 45 (1980), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Oxidation of methyl linoleate in a model emulsion system containing soy protein and copper was studied. The prooxidative effect of soy protein was inhibited following proteolysis. Both the TBA test and diene conjugation measurements showed similar oxidative patterns. The inhibitory effect of the proteolytic treatment was ascribed to the binding of copper by proteolytic products and these copper complexes appeared to be less catalytic than the intact protein-copper complex. However, the release of bound antioxidant phenolics or copper chelating agents, e.g. phytic acid following proteolysis, may also be involved.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1980.tb07525.x
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