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  • 1995-1999  (3)
  • 1990-1994  (1)
  • CRABP-I  (2)
  • 2Cys-peroxiredoxin
  • 3‐dimethy‐2‐imidazolidinone solvent system
  • 1
    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
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Molecular and cellular biochemistry 200 (1999), S. 69-76 
    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
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  • 3
    ISSN: 1573-5028
    Keywords: 2Cys-peroxiredoxin ; Chinese cabbage ; expression ; functional characterization ; gene cloning
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A cDNA (C2C-Prx) corresponding to a 2Cys-peroxiredoxin (2Cys-Prx) was isolated from a leaf cDNA library of Chinese cabbage. The predicted amino acid sequence of C2C-Prx has 2 conserved cysteines and several peptide domains present in most of the 2Cys-Prx subfamily members. It shows the highest sequence homology to the 2Cys-Prx enzymes of spinach (88%) and Arabidopsis (86%). Southern analysis using the cDNA insert of C2C-Prx revealed that it consists of a small multigene family in Chinese cabbage genome. RNA blot analysis showed that the gene was predominantly expressed in the leaf tissue of Chinese cabbage seedlings, but the mRNA was generally expressed in most tissues of mature plant, except roots. The expression of C2C-Prx was slightly induced by treatment with H2O2 (100μM) or Fe3+/O2/DTT oxidation system, but not by ABA (50 μM) or GA3 (10 μM). The C2C-Prx is encoded as a preprotein of 273 amino acids containing a putative chloroplast-targeting signal of 65 amino acids at its N-terminus. The N-terminally truncated recombinant protein (ΔC2C-Prx) migrates as a dimer in a non-reducing SDS-polyacrylamide gel and as a monomer in a reducing condition. The ΔC2C-Prx shows no immuno cross-reactivity to antiserum of the yeast thiol-specific antioxidant protein, and vice versa. The ΔC2C-Prx prevents the inactivation of glutamine synthetase and the DNA cleavage in the metal-catalyzed oxidation system. In the yeast thioredoxin system containing thioredoxin reductase, thioredoxin, and NADPH, the ΔC2C-Prx exhibits peroxidase activity on H2O2.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1058-8388
    Keywords: CRABP-I ; P19 cells ; DNA methylation ; Gene expression ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: The mouse cellular retinoic acid binding protein-I (CRABP-I) gene is specifically up-regulated by retinoic acid (RA) in P19 mouse embryonal carcinoma cells, and its expression in animals is spatially and temporally restricted to RA-sensitive tissues during embryonic development. This study demonstrates that, in adult mouse tissues and P19 cells where the expression of CRABP-I is detected at the basal level, the 5′- flanking region of the CRABP-I gene is hypermethylated at the C residues of all the Hpa II sites. Conversely, in mouse embryos during early stages of development when the expression of CRABP-I gene is detected at a much higher level, this region is demethylated at these Hpa II sites. In P19, enhancement on the RA-induced up-regulation of CRABP-I can be observed in cells treated with 5-azacytidine (5-AzaC) in conjunction with RA, where partial demethylation in the 5′-flanking region of CRABP-I gene is observed. Nuclear run-on experiments indicate that increased message levels of CRABP-I in P19 cells can be accounted for, at least partially, by increases in its transcription rates. The induction of retinoic acid receptor (RAR) β by RA can also be enhanced by 5-AzaC, but to a much lesser degree. In contrast, all the Hpa II sites in the structural gene portion, at least in the first two exons, are fully demethylated at the C residues. © 1994 Wiley-Liss, Inc.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
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