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  • 1
    Electronic Resource
    Electronic Resource
    Enzymatic Debranching of Glycogen: A New Pathway in Rabbit Muscle for the Enzymatic Debranching of Glycogen (1963)
    [s.l.] : Nature Publishing Group
    Nature 197 (1963), S. 979-980 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] A New Pathway in Rabbit Muscle for the Enzymatic Debranching of Glycogen THE breakdown of glycogen by rabbit-muscle phosphorylase is far from complete, owing to the inability of this exo-enzyme to sever or by-pass the a-l,6-branch linkages, and action normally ceases when less than 40 per cent of ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/197979a0
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  • 2
    Electronic Resource
    Electronic Resource
    Substrate Specificity of Maltose Phosphorylase (1962)
    [s.l.] : Nature Publishing Group
    Nature 196 (1962), S. 168-169 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Maltose phosphorylase has since been found in beer Lactobacilli4 and N. perflava5 and enzyme from the latter source can use 2-deoxy-D-glucose, D-glucosamine and N-acetyl-D-glucosamine instead of the glucose acceptor, giving rise to analogues of maltose. We are interested in maltose phosphorylase ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/196168a0
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  • 3
    Electronic Resource
    Electronic Resource
    Enzymic and Chemical Synthesis of the Alpha-1 : 2-Glucosidic Linkage: Chemical Synthesis (1956)
    [s.l.] : Nature Publishing Group
    Nature 178 (1956), S. 1222-1223 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] THE formation of 1 : 2-linked polymers of a-D-glucopyranose has been examined as part of our investigations of the chemical synthesis of sugar polymers1. The problem had an added interest since the occurrence of the a-1 : 2-glucosidic linkage in Nature has only been recognized very recently and the ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/1781222a0
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  • 4
    Electronic Resource
    Electronic Resource
    Action of Salivary α-Amylase on Amylopectin and Glycogen (1952)
    [s.l.] : Nature Publishing Group
    Nature 170 (1952), S. 748-749 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Fig. 1. a-i: 4-Linkages resistant to a-amylase action O, Glucose unit; , ct-1: 4-link; -~-, unhydrolysable a-l: 4-link; -*f a-l: 6-link Rabbit liver glycogen (from pregnant does) was exhaustively treated with enzyme purified by the method of Meyer et l.* and the products were fractionated ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/170748a0
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  • 5
    Electronic Resource
    Electronic Resource
    The Z-Enzyme in Amylolysis (1953)
    [s.l.] : Nature Publishing Group
    Nature 172 (1953), S. 494-494 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] WE are glad of the opportunity of commenting on the communication of Prof. Hopkins and Dr. Bird, which raises the old doubt that Z-enzyme is in fact a weak a-amylase. In our paper1 we emphasized the necessity of distinguishing Z-enzyme from a-amylase, and we concluded that the experiments there ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/172494a0
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  • 6
    Electronic Resource
    Electronic Resource
    D -Enzyme: a Disproportionating Enzyme in Potato Juice (1953)
    [s.l.] : Nature Publishing Group
    Nature 172 (1953), S. 158-158 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] D-enzyme brings about rapid disproportionation of malto-triose, -tetraose, -pentaose, -hexaose and -heptaose; but action in the case of maltose is doubtful. Glucose itself is not a substrate. The greater the molecular weight of the maltosaccharide substrate, the greater is the final intensity of ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/172158a0
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  • 7
    Electronic Resource
    Electronic Resource
    Determination of Molecular Weights of Polysaccharides by Over-oxidation with Periodate (1959)
    [s.l.] : Nature Publishing Group
    Nature 183 (1959), S. 991-992 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The requisite carbonyl groups for activation of the C H bond are found as aldehyde groups. The oxidation of the C H group creates new a-glycol centres and further oxidation (over-oxidation) ensues. The oligosaccharide is therefore slowly eroded from its reducing-end unit with the evolution of ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/183991a0
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  • 8
    Electronic Resource
    Electronic Resource
    Synthesis of Amylose by Potato D -Enzyme (1959)
    [s.l.] : Nature Publishing Group
    Nature 183 (1959), S. 46-46 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] We have preferred to use yeast hexokinase in the present experiments because it can be obtained in a better state of purity than the potato enzyme. In the first instance D-enzyme was incubated with a mixture of maltodextrins (malto-pentaose, -hexaose and -heptaose) from which some of the products ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/183046a0
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  • 9
    Electronic Resource
    Electronic Resource
    Mechanism of the Beta-Amylolysis of Amylose (1950)
    [s.l.] : Nature Publishing Group
    Nature 166 (1950), S. 258-259 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] THE mechanism by which beta-amylase degrades amylose has been the subject of recent papers by Swanson and Cori1-8 and by Cleveland and Kerr46. These authors hold the view that, during beta-amylolysis, an enzyme molecule attaches itself to an amylose molecule, and, by the stepwise removal of maltose ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/166258a0
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  • 10
    Electronic Resource
    Electronic Resource
    Birefringence of Amylose and Amylopectin in Whole Structural Starches (1950)
    [s.l.] : Nature Publishing Group
    Nature 166 (1950), S. 34-34 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] We now report further evidence relating to these problems. Wrinkled pea, smooth pea, normal maize, waxy maize, and tobacco leaf starches were examined in polarized light. Wrinkled pea starch contains 98 per cent amylose and 2 per cent amylopectin9; smooth pea contains amylose and amylopectin in the ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/166034a0
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