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  • 1975-1979  (15)
  • 1935-1939  (8)
  • 1
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Journal of the American Chemical Society 59 (1937), S. 214-215 
    ISSN: 1520-5126
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 30 (1978), S. 0 
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract— A fluorometric assay for choline acetyltransferase has been developed. This assay is based on coupling the choline acetyltransferase dependent formation of acetyl-CoA from acetylcholine and coenzyme A, to the reactions catalyzed by the enzymes citrate synthase and malic dehydrogenase. Although this assay is not as sensitive as previously described radiometric assays, it can be conveniently used during enzyme purification.Employing this assay method, choline acetyltransferase has been purified from human placenta to a specific activity of 92.7 μmol acetylcholine formed/min/mg protein.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 30 (1978), S. 0 
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract— The effects of salt on the properties of human placental choline acetyltransferase have been examined. Increases in enzyme activity, thermal denaturation and susceptibility to proteolysis can be related to increases in ionic strength, rather than to specific salt effects. Increased ionic strength increases the maximal velocity (Km) of the reaction, with no change in the kinetic parameter Vmax/Km (choline). The pH-Km profile, measured over the range of 6.5–8.0, indicates the requirement of a dissociated acidic residue whose pKa is below 7.5 at high ionic strength, and a protonated residue whose pKa is above 7.5 at low ionic strength. It is proposed that the conformation of the enzyme is different at high ionic strength and at low ionic strength, and that these different conformational states of the enzyme result in different rate-determining steps of the reaction.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 32 (1979), S. 0 
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract— The effects of monovalent and divalent anions on the choline acetyltransferase reaction have been determined at high (5.0 mM) and low (0.58 mM) choline. At 0.58 mM-choline, both monovalent and divalent anions activate the enzyme ±9 fold; however, at 5.0mM-choline, monovalent anions activate the enzyme ±25 fold, while divalent anions activate ±9 fold. Both monovalent and divalent anions show uncompetitive activation with respect to choline. When either dimethylaminoethanol, N-(2-hydroxyethyl)-N-methyl piperidinium iodide, or N-(2-hydroxyethyl)-N-propyl pyrrolidinium iodide was substituted for choline, activation by monovalent or divalent anions was only 2.5-4 fold. With AcCoA as substrate the ChA reaction can be increased ±20 fold by increased salts; however, with acetyl dephosphoCoA as substrate, the reaction is insensitive to the salt concentration. Similar salt effects on the ChA reaction, as measured in the direction of acetylcholine synthesis, have been demonstrated in the reverse reaction. In addition, inhibition of the forward reaction by acetylcholine has been measured as a function of sodium chloride concentration. Although the K1 for acetylcholine increases with increasing salt, this change in K1, parallels the increase in the Km for choline. These results support the hypothesis that both monovalent and divalent anions activate choline acetyltransferase by the same singular mechanism; which is to increase the rate of dissociation of coenzyme A from the enzyme.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 42 (1977), 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: Direct comparisons were made on the content and retention of thiamine, pyridoxine, niacin and folacin in quick-cooking (large Lima, pinto, pink, blackeye) beans prepared from authentic, chemically characterized lots of commercial dry beans. Significant losses occurring during cooking and their relationship to cooking time differentials were determined and the vitamin levels in cooked beans compared with ofher outstanding sources of B-complex vitamins. Data show dry beans are a good source of B-complex vitamins, but levels vary considerably with bean type and processing/cooking methods. Cooked, quick-cooking Lima and blackeye beans had slightly higher levels of all four vitamins than standard cooked beans, but standard cooked pink and pinto had higher levels of thiamine, pyridoxine and niacin; folacin differences were inconsistent. There was no consistent relationship between vitamm content and cooking time. Cooked blackeye, large Lima and pink were equivalent or higher than beef liver or wheat germ with respect to thiamine, better sources of pyridoxine than yeast or wheat germ, but lower in niacin than liver. With respect to folacin, blackeye beans are a better source than liver, wheat germ or yeast and large Lima and pink are equal or better than beef liver or yeast.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 246 (1975), S. 0 
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 246 (1975), S. 0 
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 44 (1979), 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: A simple, practical procedure has been developed for the preparation of quick-cooking winged beans. In boiling water the raw processed beans tenderized within 20 min or about 10% of the time required to cook untreated, pre-soaked beans. Redried, processed beans required about 45 min to cook without pre-soaking. The cooked, quick-cooking products had a smooth uniform texture, excellent whole bean appearance and enhanced natural flavor. In comparison with soybean, with which they have much in common, the winged beans had a more pleasing and acceptable flavor. There were only nominal differences between cooked standard and quick-cooking beans in respect to proximate composition, riboflavin, niacin and important nutrient elements. The quick-cooking process should find applications in fuel-deficient areas of the world in which dry winged bean seeds are produced or imported as a stable, high protein food commodity.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Journal of the American Chemical Society 98 (1976), S. 865-867 
    ISSN: 1520-5126
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Journal of the American Chemical Society 60 (1938), S. 1918-1924 
    ISSN: 1520-5126
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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