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  • 1995-1999  (2)
  • 3‐dimethy‐2‐imidazolidinone solvent system  (1)
  • CRABP-I  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Reaction characteristics of cellulose in the LiCl/1,3‐dimethyl‐2‐imidazolidinone solvent system (1999)
    Springer
    Cellulose 6 (1999), S. 93-102 
    Details
    ISSN: 1572-882X
    Keywords: LiCl/1 ; 3‐dimethy‐2‐imidazolidinone solvent system ; homogeneous cellulose solution ; cellulose acetate ; O‐methylcellulose ; reaction characteristics
    Source: Springer Online Journal Archives 1860-2000
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract In order to elucidate the nature of the LiCl/1,3‐dimethy‐2‐imidazolidinone (DMI) solvent system as one of the homogeneous reaction media of cellulose, cellulose acetate (CA) and O‐methylcellulose (MC) were prepared using this solvent system, and the distribution of substituents within anhydroglucose units was examined by 13C‐NMR. It was found that (i) homogeneous cellulose solutions can be easily prepared by heating 2, 5–12 and 100 parts of weight of cellulose, LiCl, and DMI, respectively, and (ii) the relative reactivity of hydroxyl groups is in the order C‐6 〉 C‐2 〉 C‐3 for both CA and MC. A remarkable feature of this solvent system is that the reaction efficiency in etherification is very high compared with other homogeneous solvent systems.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1009208417954
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Studies of the type I cellular retinoic acid-binding protein mutants and their biological activities (1999)
    Springer
    Molecular and cellular biochemistry 200 (1999), S. 69-76 
    Details
    ISSN: 1573-4919
    Keywords: CRABP-I ; RA induction ; RA binding ; mutagenesis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract We have mutated the type I cellular retinoic acid binding protein (CRABP-I), individually at the Arg131 (into Ala) and the Tyr 133 (into Phe) residues which have been predicted to make direct contact with retinoic acid (RA) based upon previous structural studies. The RA-binding affinities of these mutants are examined and their biological effects on RA induction of reporter genes are determined. The R131A mutation drastically affects its ligand-binding property, but the Y133F mutation has little effect. By using an RA-inducible reporter, it is found that the wild type CRABP-I exerts biphasic effects on RA induction of the reporter. The early (at 12 h) effect is to enhance RA induction, whereas the delayed (at 24 h) effect is to suppress RA induction. In consistence with their RA binding property, the R 131A mutant loses both its early and delayed biological activities, whereas the Y133F mutant remains as effective as the wild type. It is concluded that CRABP-I over-expression exerts biphasic effects on RA-mediated gene expression, and that Arg131, but not Tyr 133, is essential for a high RA-binding affinity of this protein as well as its biological activity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006906415388
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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