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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Science Ltd
    International journal of cosmetic science 26 (2004), S. 0 
    ISSN: 1468-2494
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Collagen is an important component for cosmetic formulation, where it is an effective natural humectant with high substantivity. Commercial collagen preparations have a wide range of properties. In the present study, various techniques have been used to examine three distinct commercial collagens that illustrate the range of properties that are available. The usefulness of the various techniques for assessing collagen quality and batch-to-batch variation is discussed. The results indicate that there are several simple, cheap and effective methods such as gel electrophoresis that provide excellent information on collagen quality. The appropriate selection of tests allows informed decisions on the choice of which collagen preparation to use in providing the desired functionality and shelf life of a formulation.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 228 (1970), S. 552-554 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] There are two principal methods for the mathematical treatment of sequence data from a large number of species3'4. The matrix method (for example ref. 5) is used to construct a tree so that the reconstructed matrix derived from it is the closest approximation to the original matrix obtained from ...
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The three-dimensional structure of plastocyanin, a ‘blue’ or ‘Type 1’ copper-protein, has been determined at a resolution of 2.7 Å. The copper atom has a highly distorted tetrahedral coordination geometry. It is coordinated by a cysteine thiol group, a methionine ...
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1573-4927
    Keywords: Drosophila melanogaster ; D. hydei ; D. immigrans ; D. mercatorum ; glycerol-3-phosphate dehydrogenase ; peptide mapping ; amino acid sequencing
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract This report describes preliminary protein structural studies of glycerol-3-phosphate dehydrogenase (α-GPDH) fromDrosophila spp. and an important innovative feature of our enzyme purification protocol. The scheme involves the coupling of substrate (α-glycerophosphate) elution from CM-Sephadex and cofactor (NADH) elution from Affi-Gel blue resin. Using this method a 32.7% yield and a 111-fold purification were obtained from aD. melanogaster line carrying the α-Gpdh S allele at the α-Gpdh locus. The product obtained from 0 to 3-day-old adult flies was electrophoretically homogeneous and consisted mainly of the adult α-GPDH-1 isozyme. The method was used to obtain α-GPDH protein fromD. melanogaster (two lines),D. hydei, D. immigrans, andD. mercatorum. Peptide mapping revealed structural differences among the enzymes from the different species, and amino acid sequencing showed many similarities betweenD. melanogaster α-GPDH and the rabbit muscle enzyme.
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 1573-4927
    Keywords: Drosophila melanogaster ; D. hydei ; D. immigrans ; D. mercatorum ; glycerol-3-phosphate dehydrogenase ; peptide mapping ; amino acid sequencing
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract This report describes preliminary protein structural studies of glycerol-3-phosphate dehydrogenase (α-GPDH) fromDrosophila spp. and an important innovative feature of our enzyme purification protocol. The scheme involves the coupling of substrate (α-glycerophosphate) elution from CM-Sephadex and cofactor (NADH) elution from Affi-Gel blue resin. Using this method a 32.7% yield and a 111-fold purification were obtained from aD. melanogaster line carrying the α-Gpdh S allele at the α-Gpdh locus. The product obtained from 0 to 3-day-old adult flies was electrophoretically homogeneous and consisted mainly of the adult α-GPDH-1 isozyme. The method was used to obtain α-GPDH protein fromD. melanogaster (two lines),D. hydei, D. immigrans, andD. mercatorum. Peptide mapping revealed structural differences among the enzymes from the different species, and amino acid sequencing showed many similarities betweenD. melanogaster α-GPDH and the rabbit muscle enzyme.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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