Library

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    Electronic Resource
    Electronic Resource
    Dutch legislation (1986)
    [s.l.] : Nature Publishing Group
    Nature 321 (1986), S. 556-556 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] SIR-Your leading articles have frequently highlighted developments in the United States and the United Kingdom concerning ethical and legal aspects of the use of animals in research. New regulations, based on the 1977 Act of Animal Experimentation, recently became effective in the Netherlands. ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/321556b0
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Biochemical polymorphism in the rat: Genetics of three electrophoretic variants and characterization of inbred strains (1981)
    Springer
    Biochemical genetics 19 (1981), S. 173-186 
    Details
    ISSN: 1573-4927
    Keywords: genetics ; electrophoresis ; biochemical polymorphism ; strain characterization ; rat
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Nine inbred strains of the rat (Rattus norvegicus) were screened for differences in electrophoretically detectable proteins. Interstrain variation was observed for 7 of 26 proteins. Three of these variants have not been described previously: leucine aminopeptidase (Lap-1), major urinary protein (Mup-1), and seminal vesicle protein (Svp-2). Genetic analysis revealed two autosomal alleles for each of these polymorphisms. The loci Lap-1, Mup-1, and Svp-2 are linked neither to one another nor to the previously described Svp-1 and Es-4 loci. Each of the nine strains can be identified now by a specific set of monogenic markers.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00486146
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Serum esterase genetics in rabbits. III. A third allele on the Est-2 locus (1975)
    Springer
    Biochemical genetics 13 (1975), S. 19-28 
    Details
    ISSN: 1573-4927
    Keywords: esterases ; genetics ; rabbit
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract A fast-migrating F' zone of the prealbumin serum esterase system of rabbits is demonstrated in low frequency in the breed Vienna White (stock Cpb:VW). Evidence is given that this zone is controlled by a third allele of the Est-2 locus. The zymotypic expression of this allele (Est-2 F′) shows codominance in combination with the Est-2 F allele and complete dominance in combination with the Est-2 f′ allele. In contradistinction to the F zones of the Est-2 F allele, the F′ zone possesses no atropinesterase activity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00486003
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 4
    Electronic Resource
    Electronic Resource
    Separation of β-d-galactosidases in rabbit tissues: Genetics of neutral β-d-galactosidase (1983)
    Springer
    Biochemical genetics 21 (1983), S. 177-189 
    Details
    ISSN: 1573-4927
    Keywords: β-d-galactosidase ; β-d-glucosidase ; electrophoresis ; genetics ; rabbit
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Three different types of β-d-galactosidase (EC 3.2.1.23) could be distinguished in rabbit tissues using electrophoretic procedures. (1) Acid β-d-galactosidase with a low mobility and maximal activity at pH 3–5 was found in the particulate fraction of various tissue homogenates. This enzyme hydrolyzed 4-methylumbelliferyl-d-galactoside, but no activity against other glycoside substrates could be demonstrated. The enzyme was inhibited by galactono-(1 → 4)-lactone. (2) Lactose-hydrolyzing β-d-galactosidase with an intermediate mobility was found only in juvenile small intestine. Most of the activity was found in the particulate fraction of the cell. The enzyme hydrolyzed several other synthetic glycoside substrates besides lactose. It was most active at pH 5–6 and strongly inhibited by glucono-(1 → 5)-lactone but not much affected by galactono-(1 → 4)-lactone. (3) Neutral β-d-galactosidase with a fast mobility and maximal activity at pH 6–8 was found in the soluble fraction of homogenates from liver, kidney, and small intestine. This enzyme also showed a broad substrate specificity; it possessed activity against aryl-β-d-glucoside, -fucoside, and -galactoside substrates but not against lactose. The enzyme was strongly inhibited by glucono-(1 → 5)-lactone and (less) by galactone-(1 → 4)-lactone. Neutral β-d-galactosidase and neutral β-d-glucosidase (EC 3.2.1.21) are probably identical enzymes in the rabbit. Individual variation, in both electrophoretic mobility and activity, was found for neutral β-d-galactosidase. Genetic analysis of the electrophoretic variants revealed that two alleles at an autosomal locus are responsible for this variation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00000016
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 5
    Electronic Resource
    Electronic Resource
    Specific effect of the amount of dietary fat on esterase-1 (ES-1) activity of rat plasma (1990)
    Springer
    European journal of nutrition 29 (1990), S. 129-134 
    Details
    ISSN: 1436-6215
    Keywords: rat ; dietaryfat ; esterase-1 (ES-1) ; plasma ; Ratte ; diätetischesFett ; Esterase-1 (ES-1) ; Plasma
    Source: Springer Online Journal Archives 1860-2000
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Medicine
    Description / Table of Contents: Zusammenfassung Die Frage, die sich stellt, ist: Beeinflußt die Zunahme von Nahrungsfett die Esterase-1-Aktivität (ES-1) im Plasma von Ratten mehr als Kohlenhydrate oder Proteine? Es wurde daher bei männlichen Ratten der Effekt auf die Esterase-1-Aktivität durch das Austauschen des Nahrungsfettes mit isokalorischen Mengen an Kohlenhydraten und Proteinen bestimmt. In hoch fetthaltigem Futter erreichte Maisöl höhere Esterase-1-Aktivität im Plasma von Ratten als Kokosnußöl. Die Esterase-1-Aktivität war abnehmend bei erniedrigter Fettaufnahme. Das Austauschen des Nahrungsfettes durch Kohlenhydrate oder Proteine produziert die gleiche Abnahme der Esterase-1-Aktivität im Plasma. Dagegen tritt keine nennenswerte Veränderung der Esterase-1-Aktivität beim Austausch von Kohlenhydraten mit Proteinen auf. Daraus folgt, daß die Höhe des Fettgehalts in der Nahrung die Esterase-1-Aktivität beeinflußt.
    Notes: Summary The question addressed is whether the amount of dietary fat rather than that of carbohydrates or protein affects esterase-1 (ES-1) activity in plasma of rats. For this purpose, the effects on plasma ES-1 activity of replacement of dietary fat, by isocaloric amounts of either carbohydrates or protein were studied in male rats. In rats fed high-fat diets, corn oil induced higher plasma ES-1 activities than coconut fat. Plasma ES-1 activity was decreased by a decrease in fat intake. Replacement of fat by carbohydrates produced a similar decrease of plasma ES-1 activity as did replacement of fat by protein. Replacement of carbohydrates by protein did not significantly change plasma ES-1 activity. It is concluded that the amount of fat in the diet specifically influences ES-1 activity in plasma.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02021668
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 6
    Electronic Resource
    Electronic Resource
    Serum esterase genetics in rabbits. IV. The prealbumin and β-globulin systems (1977)
    Springer
    Biochemical genetics 15 (1977), S. 989-1000 
    Details
    ISSN: 1573-4927
    Keywords: genetics ; esterases ; evolution ; rabbit ; mouse
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Discontinuous starch gel electrophoresis revealed a fourth allele of rabbit prealbumin serum esterase at locus Est-2. This allele is designated Est-2 f and appears to be silent. In addition to the prealbumin serum esterases, another serum esterase system was studied in rabbits. This system is localized in the β-globulin region. Genetic analysis indicated that one locus with two codominant alleles controls the variation in this region. Linkage of this system with Est-1 and Est-2 of the prealbumin serum esterases was demonstrated. Comparison of the arrangement of these esterase loci on linkage group VI with the esterase loci on chromosome 8 of the mouse gives additional support for the theory of evolutionary conservation of chromosomal segments coding for mammalian esterases.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00483993
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 7
    Electronic Resource
    Electronic Resource
    Serum esterase genetics in rabbits. I. Phenotypic variation of the prealbumin esterases and classification of atropinesterase and cocainesterase (1974)
    Springer
    Biochemical genetics 12 (1974), S. 309-326 
    Details
    ISSN: 1573-4927
    Keywords: atropinesterase ; cocainesterase ; enzyme classification ; phenotypic variation ; rabbit
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Rabbit atropinesterase and cocainesterase were studied by starch gel electrophoresis. The enzymes are localized in a region of the gels anodal to the albumins (prealbumin esterases). In this region, three groups of esterase zones (S, F, and D) can be distinguished. The S and F zones are almost exclusively responsible for the hydrolysis of cocaine and atropine, respectively. There is an interdependence of the S, F, and D zones: the activity of zone D depends on the presence of the three F zones, whereas these F zones are found only in combination with the three S zones. α-Naphthylacetate as a substrate reveals six different phenotypes; two of these phenotypes are shown to be composed of two subtypes when a supplementary staining procedure is executed. Atropinesterase and cocainesterase are classified as carboxylesterases (E.C. 3.1.1.1.) with a rather wide specificity for both aliphatic and aromatic esters. The α-naphthol esters are split better than the corresponding β-naphthol esters. Naphthol esters with an acyl side-chain of three carbon atoms are hydrolyzed optimally by the enzymes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00485951
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 8
    Electronic Resource
    Electronic Resource
    Genetics of a tissue esterase polymorphism (Est-6) in the rabbit (Oryctolagus cuniculus) (1987)
    Springer
    Biochemical genetics 25 (1987), S. 335-344 
    Details
    ISSN: 1573-4927
    Keywords: esterase ; genetics ; homology ; rabbit
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Genetic analysis of a polymorphic tissue esterase revealed a new locus (Est-6) with two alleles (Est-6 a andEst-6 b) on linkage group VI of the rabbit.Est-6 is closely linked to theEst-1,2,4 cluster. Esterase ofEst-6 is found in many organs, particularly in liver and small intestine, but not in erythrocytes and serum.Est-6 esterase hydrolyzes α-naphthyl acetate and butyrate, naphthol AS-D acetate, indoxyl acetate, and butyrate as well as 5-bromoindoxyl acetate,N-acetyl-l-alanine-α-naphthyl ester but not 4-methylumbelliferyl acetate and fluorescein diacetate. The enzyme is inhibited by bis-p-nitrophenyl phosphate and eserine but not byp-chloromercuribenzoate. It was classified as a carboxylesterase (EC 3.1.1.1). Based on chromosomal localization, tissue distribution, substrate specificity, inhibitor sensitivity, and range ofpI's, rabbitEst-6 is assumed to be homologous with mouseEs-7.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00554543
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 9
    Electronic Resource
    Electronic Resource
    Heterogeneity of Es-1 esterases in the rabbit (Oryctolagus cuniculus) (1984)
    Springer
    Biochemical genetics 22 (1984), S. 853-870 
    Details
    ISSN: 1573-4927
    Keywords: esterase ; genetics ; rabbit
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Analysis of the Es-1 system in the rabbit with polyacrylamide gel electrophoresis (PAGE) revealed a high degree of individual variation. In the liver the number of esterase bands found in the Es-1 region of the gels ranged from 2 to 16. The results indicate that one locus with three alleles is responsible for all of the esterase bands in the Es-1 region. The most plausible explanation for the observed heterogeneity is that each of the alleles codes for a protein (MW 65,000±2000) that is changed by posttranslational modifications, thus giving rise to two to five monomeric enzymes with esterase activity. Polymerization of these monomers then results in 1–11 dimers. Based on similarities with mouse Es-9, chromosomal homology between rabbit Es-1 and mouse Es-9 is proposed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00499477
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 10
    Electronic Resource
    Electronic Resource
    Assignment of Lap-1 to linkage group I of the rat (Rattus norvegicus) (1985)
    Springer
    Biochemical genetics 23 (1985), S. 599-606 
    Details
    ISSN: 1573-4927
    Keywords: rat ; leucine arylaminopeptidase ; linkage
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Genetic analysis of backcross progeny from previously characterized rat inbred strains revealed that the biochemical marker Lap-1 is localized in linkage group I (LG I). Lap-1 codes for leucine arylaminopeptidase (EC 3.4.11). The distances of Lap-1 to c, RT6, and Hbb, based on recombination frequencies, are 3.1±1.5, 8.3±4.0, and 11.4±2.8 cM, respectively. Acon-1 codes for aconitase (EC 4.2.1.3). The calculated distances of Acon-1 to c and Hbb are 30.1±5.0 and 36.1±5.3 cM, respectively. This suggests that Acon-1 is also in LG I, but the observed high frequency of double crossovers requires further confirmation of this linkage. Ahd-2, Es-6, and Gdc-1 are linked neither to markers of LG I nor to one another.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00504294
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...