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  • Electronic Resource  (40)
  • 1980-1984  (40)
  • 1950-1954
  • 11
    Electronic Resource
    Electronic Resource
    Shikimate-derived metabolites. 11. A total synthesis of (.+-.)-chorismic acid (1982)
    s.l. : American Chemical Society
    Journal of the American Chemical Society 104 (1982), S. 6787-6788 
    Details
    ISSN: 1520-5126
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/ja00388a055
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  • 12
    Electronic Resource
    Electronic Resource
    High and low temperature tolerances and their relationships to distribution of agaves (1983)
    Oxford, UK : Blackwell Publishing Ltd
    Plant, cell & environment 6 (1983), S. 0 
    Details
    ISSN: 1365-3040
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract. The potential influence of tissue tolerances to extreme temperatures on distributional limits was investigated for 15 taxa (14 species) of leaf-succulent agaves from the south-western United States and northern Mexico. As a group, the agaves exhibited a moderate low temperature tolerance of – 11°C (based on a 50% inhibition in the number of mesophyll cells taking up a stain, neutral red). However, nearly all of the species were able to tolerate extremely high tissue temperatures of over 60°C. Nocturnal acid accumulation by these crassulacean acid metabolism plants was about 6°C more sensitive to temperature extremes than was cellular membrane integrity.High and low temperature acclimation in response to changing day/night air temperatures was observed in all 15 taxa, with high temperature acclimation averaging two-fold greater than low temperature acclimation (3.8°C versus 2.0°C per 10°C change in ambient temperature). Species occupying the coldest habitats exhibited the greatest low temperature tolerances and acclimation; several such species, such as Agave utahensis and A. schottii, had small rosette sizes which resulted in higher minimum leaf temperatures. Species from the hottest habitats had among the greatest high temperature tolerances and acclimation; the two species from open desert scrub habitats, A. deserti and A. lecheguilla, had the lowest leaf shortwave absorptances observed, which would result in lower maximum leaf temperatures. Thus morphology and tissue tolerances to stressful temperatures reflect the temperature extremes of a plant's native habitat, although low temperature tolerance appears to limit the distribution of agaves more than high temperature tolerance.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/1365-3040.ep11589339
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  • 13
    Electronic Resource
    Electronic Resource
    ROLE OF NITRITE IN CURED MEAT FLAVOR: SENSORY ANALYSIS (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: The effect of varying levels of nitrite on the development of cured meat flavor in hams was investigated. Sensory evaluation studies demonstrated that concentrations of sodium nitrite as low as 50 mg/kg developed a significant (p 〈 0.05) cured meat flavor. In addition, this level of nitrite was as equally effective as 500 mg/kg of nitrite in retarding the development of off-odors and flavors during aerobic storage of hams for 7 days at 4°C. Reduced off-flavor formation was also observed in meat samples. treated with 0.02% butylated hydroxytoluene or 1000 mg/kg of citric acid although these compounds were not as effective as 50 mg/kg of nitrite in producing a typical ham aroma or flavor. The intensity of cured meat aroma/flavor as well as overall palatability was found to be directly related to a decrease in off-odors/flavors present in the product.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1980.tb07471.x
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  • 14
    Electronic Resource
    Electronic Resource
    Differential Scanning Calorimetry of Beef Muscle: Influence of Postmortem Conditioning (1984)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 49 (1984), 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: Differential scanning calorimetry (DSC) was used to follow the changes in the endothermic transitions of beef muscle during conditioning. Sternomandibularis muscle held at 5°C from 2–8 days postmortem resulted in a significant (P 〈 0.05) drop in the total heat of transition (ΔH) from 3.8 to 3.0 J/g. The myosin transition decreased from 57.8° to 55.2°C while the actin transition increased from 81.8° to 83.2°C (P 〈 0.05). Storage time and temperature were varied to generate a response surface of thermal data for psoas major and semimembraneosus muscle. The decrease in °H of psoas major was optimal between 10° and 13°C. Total ΔH of semimembraneosus (3.9 J/g) was significantly greater (P 〈 0.05) than that of psoas major (3.4 J/g).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1984.tb12833.x
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  • 15
    Electronic Resource
    Electronic Resource
    Differential Scanning Calorimetry of Beef Muscle: Influence of Sarcomere Length (1984)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 49 (1984), 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: Contraction state of beef muscle at onset of rigor influences tenderness of cooked meat. Loss in tenderness during cooking has been related, through use of differential scanning calorimetry (DSC), to thermal denaturation of myofibrillar proteins. Contraction of beef sternomandibularis muscle was controlled at sarcomere lengths of 2.4, 2.1, 1.9, 1.7, and 1.4 μm. Samples were scanned from 25- 105°C at 10°C/min; ΔH (change in heat of transition) between 45° and 92°C dropped from ca. 4 J/g muscle at 2.4 μm to ca. 3 J/g at 1.4 μm. This difference (P 〈 0.05) amounts to less than 1% of the total energy resuired to heat meat from 45° to 92°C. The decrease is attributed to a greater actomyosin contribution to the overall thermal curve resulting from increased overlap of the filaments.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1984.tb12837.x
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  • 16
    Electronic Resource
    Electronic Resource
    The Shifting of FHA Discount Points: Actual Vs. Expectations (1984)
    Oxford, UK : Blackwell Publishing Ltd
    Real estate economics 12 (1984), S. 0 
    Details
    ISSN: 1540-6229
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Economics
    Notes: This study extends the earlier studies by Zerbst and Brueggeman (Z&B) and Colwell, Guntermann and Sirmans (CGS) with regard to the shifting of FHA discount points by the seller to the buyer in the form of a higher selling price. The study extends the earlier studies by reducing the estimation problems of the CGS model and further developing the Z&B model to incorporate expected discount points built into the asking price. The results presented indicate that 100% of the points are not being shifted. Reasons for the less-than-full shifting are given.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/1540-6229.00315
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  • 17
    Electronic Resource
    Electronic Resource
    Analgesic Properties and Effects on Striatal Enkephalin Levels of Inhibitors of Membrane-Bound Metalloendopeptidase (1984)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 435 (1984), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1984.tb13852.x
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  • 18
    Electronic Resource
    Electronic Resource
    PROTEIN-PHYTATE INTERACTIONS IN SOYBEANS. I. LOCALIZATION OF PHYTATE IN PROTEIN BODIES AND GLOBOIDS (1982)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food biochemistry 6 (1982), S. 0 
    Details
    ISSN: 1745-4514
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: A study was made of whole soybeans, isolated protein bodies and a fraction consisting of globoid inclusions separated from protein bodies by centrifugation in order to observe the cellular location of phytate and to determine any indication of protein-phytate interaction within the soybean cell. Microstructural and chemical evidence demonstrated phytic acid to be located in the protein bodies of the soybean, likely in the form of a soluble protein-phytate salt with significant amounts specifically deposited in globoid inclusions. The probable existence of a protein-cation-phytate complex in situ was shown by gel filtration in which calcium and phosphorus was found to coelute with soluble proteins. The proteins involved in this interaction were tentatively identified as the 7S soybean fraction.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1745-4514.1982.tb00305.x
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  • 19
    Electronic Resource
    Electronic Resource
    PROTEIN-PHYTATE INTERACTION IN SOYBEANS. III. THE EFFECT OF PROTEIN-PHYTATE COMPLEXES ON ZINC BIOAVAILABILITY (1982)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food biochemistry 6 (1982), S. 0 
    Details
    ISSN: 1745-4514
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: A study was conducted to determine the influence of pH on the chemical form of phytate in a commercial soy isolate and its effect on zinc bioavailability by monitoring weight gain in weanling rats. Ultrafiltration studies demonstrated that the free phytate content of soy isolate solutions was greatest at pH 5.0; above this the neutralization of soy isolates resulted in the formation of a soluble proteinphytate complex. The bioavailability of zinc from diets providing protein from egg, acid and neutral soy isolates and containing various levels of added zinc was measured. The growth of rats receiving zinc from the neutral soy isolate was significantly lower than that of rats deriving zinc from either the acidic soy isolate or egg white diets. It is proposed that the reduction in bioavailability of zinc caused by the neutralization of soy protein isolate is related to the formation of a protein-zinc-phytic acid complex resistant to hydrolysis in vivo.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1745-4514.1982.tb00307.x
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  • 20
    Electronic Resource
    Electronic Resource
    PROTEIN-PHYTATE INTERACTIONS IN SOYBEANS. II. MECHANISM OF PROTEIN-PHYTATE BINDING AS AFFECTED BY CALCIUM (1982)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food biochemistry 6 (1982), S. 0 
    Details
    ISSN: 1745-4514
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Phytate and bovine serum albumin were used in a model system to investigate the mechanism of their binding. Ultrafiltration studies using response surface design showed the association of protein and phytic acid to be highly pH dependent. Under acid conditions, the protein formed an insoluble complex with phytic acid. At pH 3.0, a binding constant of 2.3 times 105 was obtained and it was calculated that there are 78 binding sites of the total 93 basic amino acid residues potentially available. This low pH complex was not disrupted at high temperatures but the presence of calcium ions caused dissolution of the precipitate. Calcium produced different effects at higher pH (〉 6). Soluble protein-calcium-phytic acid complexes were formed which were less stable to heat and dissociated above pH 10 at high ionic strength. Since this interaction occurred only in the presence of calcium, a salt linkage is implicated in which divalent cations simultaneously bind to the protein and phytic acid in the form of a soluble complex. It is proposed that either the addition of divalent cations at low pH or sequestering agents at high pH would best effect the removal of phytate from soy products by ultrafiltration.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1745-4514.1982.tb00306.x
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