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  • urea-cycle enzymes  (2)
  • electron microscopy  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Effects of deletions in mouse chromosome 7 on expression of genes encoding the urea-cycle enzymes and phosphoenolpyruvate carboxykinase (GTP) in liver, kidney, and intestine (1988)
    Springer
    Biochemical genetics 26 (1988), S. 769-781 
    Details
    ISSN: 1573-4927
    Keywords: urea-cycle enzymes ; phosphoenolpyruvate carboxykinase ; hepatocyte development ; tissue-specific gene expression ; mutant mice
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Chromosomal deletions at and around the albino locus on chromosome 7 of the mouse affect the enzyme activities and steady-state levels of mRNAs for five urea-cycle enzymes in liver. In newbornc 3H homozygotes, activities of these enzymes were 43–62% of normal, while corresponding mRNA levels were 14–29% of normal.c 14CoS deletion homozygotes expressed mRNA levels for these enzymes which were 32–48% of normal. However, transcription rates of these genes in hepatic nuclei ofc 3H/c3H mice were reduced only to 57–84% of normal. Since effects of the deletions had previously been noted in the kidney, mRNA levels for three enzymes expressed also in the kidney were examined. Mice homozygous for thec 3H deletion, shown previously to have drastically reduced mRNA levels for phosphoenolpyruvate carboxykinase in the liver, expressed the same deficiency in the kidney, while mRNA levels for argininosuccinate synthetase and argininosuccinate lyase were reduced in the liver but remained unaffected in the kidney. However, mRNA levels for phosphoenolpyruvate carboxykinase, carbamyl phosphate synthetase I, and ornithine transcarbamylase were unaffected in the intestine ofc 3H homozygotes. The results suggest that a regulatory factor(s) encoded in the DNA encompassed by the deletion is involved in the normal developmental maturation of hepatocytes and certain cells in the kidney.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00553875
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  • 2
    Electronic Resource
    Electronic Resource
    Effects of deletions in mouse chromosome 7 on expression of genes encoding the urea-cycle enzymes and phosphoenolpyruvate carboxykinase (GTP) in liver, kidney, and intestine (1988)
    Springer
    Biochemical genetics 26 (1988), S. 769-781 
    Details
    ISSN: 1573-4927
    Keywords: urea-cycle enzymes ; phosphoenolpyruvate carboxykinase ; hepatocyte development ; tissue-specific gene expression ; mutant mice
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Chromosomal deletions at and around the albino locus on chromosome 7 of the mouse affect the enzyme activities and steady-state levels of mRNAs for five urea-cycle enzymes in liver. In newbornc 3H homozygotes, activities of these enzymes were 43–62% of normal, while corresponding mRNA levels were 14–29% of normal.c 14CoS deletion homozygotes expressed mRNA levels for these enzymes which were 32–48% of normal. However, transcription rates of these genes in hepatic nuclei ofc 3H/c3H mice were reduced only to 57–84% of normal. Since effects of the deletions had previously been noted in the kidney, mRNA levels for three enzymes expressed also in the kidney were examined. Mice homozygous for thec 3H deletion, shown previously to have drastically reduced mRNA levels for phosphoenolpyruvate carboxykinase in the liver, expressed the same deficiency in the kidney, while mRNA levels for argininosuccinate synthetase and argininosuccinate lyase were reduced in the liver but remained unaffected in the kidney. However, mRNA levels for phosphoenolpyruvate carboxykinase, carbamyl phosphate synthetase I, and ornithine transcarbamylase were unaffected in the intestine ofc 3H homozygotes. The results suggest that a regulatory factor(s) encoded in the DNA encompassed by the deletion is involved in the normal developmental maturation of hepatocytes and certain cells in the kidney.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02395522
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  • 3
    Electronic Resource
    Electronic Resource
    Actin filament structure probed with monoclonal antibodies (1993)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 25 (1993), S. 73-86 
    Details
    ISSN: 0886-1544
    Keywords: F-actin ; monoclonal antibody ; epitopes ; electron microscopy ; structure ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The interaction of two monoclonal antibodies (mAbs) with actin has been characterized to map the epitopes defined by these mAbs and to determine the accessibility of these sites in the actin filament (F-actin). Both mAbs react specifically with actin in radioimmunoassays and Western blot assays, and by immunoprecipitation. The location of the epitopes within the primary structure of actin has been determined using limited proteolysis of actin and Western blots, or using immunoprecipitation of truncated actin fragments synthesized in a cell free translation assay. Both mAbs bind to the C-terminal fragment of actin (residues 68-375) produced by chymotrypsin cleavage. One epitope is further localized to a 9.9 kD peptide corresponding to residues 5-93. Therefore, the epitope defined by this mAb (2G11.4) lies between residues Lys68 and Glu93 of actin. The location of the other epitope was determined by immunoprecipitation of actin fragments synthesized in vitro. Removal of residues 356-365 from the C-terminus of actin completely abolished the binding of mAb 4E3.adl. Therefore, this mAb defines an epitope that involves residues between Trp356 and Ala365. The accessibility of these epitopes in native F-actin was determined with solution binding assays and characterized by immunoelectron microscopy. Monoclonal antibody 4E3.adl binds strongly to filaments, resulting in bundling or decoration of F-actin depending on the valency of the mAb, and indicating that the epitope is readily accessible in F-actin. In contrast, mAb 2G11.4 disrupts F-actin structure, resulting in the formation of an amorphous immunoprecipitate. These results place constraints on models of actin filament structure. © 1993 Wiley-Liss, Inc.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970250109
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