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  • 1985-1989  (5)
  • serum polymorphism  (3)
  • α-l-fucosidase  (3)
  • C57BL/6J mice  (2)
  • 1
    Electronic Resource
    Electronic Resource
    Fixed-ratio schedules of oral ethanol self-administration in inbred mouse strains (1988)
    Springer
    Psychopharmacology 96 (1988), S. 431-436 
    Details
    ISSN: 1432-2072
    Keywords: Ethanol self-administration ; Operant behavior ; C57BL/6J mice ; BALB/cJ mice ; Fixed-ratio schedules ; Behavior genetics
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Previous studies of ethanol reinforcement in BALB/cJ and C57BL/6J mice have shown that over a range of concentrations oral ethanol appeared to serve as a reinforcer only for the C57BL/6J mice. In the previous studies BALB/cJ mice maintained rates of responding for ethanol that only slightly exceeded the rates maintained by the vehicle, water. However, the quantity of ethanol consumed with the continuous reinforcement schedule (fixed ratio one) may have led to pharmacologically significant effects, given the high sensitivity to ethanol of this genotype. The present study tested whether and to what extent ethanol would maintain responding under increasing fixed ratio size in these two strains of mice at ethanol concentrations of 0%, 8%, and 16% (w/v). For the C57BL/6J mice, as fixed-ratio size increased from 1 to 2, 4, and 8, there were almost directly proportional increases in response rate at ethanol concentrations of 8% and 16% (w/v), but not at 0%. Post-session blood ethanol levels confirmed intake of pharmacologically significant quantities. The volume consumed per unit of body weight decreased as fixed-ratio size increased. For the BALB/cJ mice, at no condition did ethanol maintain responding at levels that significantly exceeded vehicle maintained responding. BALB/cJ mice did not differ from C57BL/6J mice as fixed-ratio size was increased during vehicle conditions. These results, along with earlier findings, demonstrate that ethanol can serve as a reinforcer for C57BL/6J mice but not in BALB/cJ mice over a range of schedule conditions. They further support the conclusion that genotype is an important determinant of ethanol reinforced behavior.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02180019
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    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Biosynthesis, processing, and extracellular release of α-l-fucosidase in lymphoid cell lines of different genetic origins (1988)
    Springer
    Biochemical genetics 26 (1988), S. 401-420 
    Details
    ISSN: 1573-4927
    Keywords: α-l-fucosidase ; lymphoid cells ; fucosidosis ; serum polymorphism
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract In humans, the quantity of α-l-fucosidase in serum is determined by heredity. The mechanism controlling levels of the enzyme in serum is unknown. Lymphoid cell lines derived from individuals with either low, intermediate, or high α-l-fucosidase in serum were established. Steady-state levels of intracellular and extracellular α-l-fucosidase as well as rates of synthesis and secretion of enzyme overlapped among the cell lines. Thus,vivo} serum phenotypes were not expressed in this system. No appreciable differences in the qualitative processing of newly made α-l-fucosidase were observed among these lymphoid cell lines. Cells pulse-labeled with35S-methionine from 0.25 to 2 hr had an intracellular form of enzyme with aM r=58,000. Cells pulsed for 1.5 hr and chased for 21 hr with unlabeled methionine had an intracellular form ofM r=60,000 and an extracellular form ofM r=62,000. All three enzyme forms were glycoproteins with a common polypeptide chain ofM r=52,000 but with different carbohydrate moieties. No evidence for a high molecular mass precursor form of α-l-fucosidase was found. Fucosidosis is a rare, inherited disease in which α-l-fucosidase activity in tissues and body fluids is low or absent. The mutations for fucosidosis and the serum polymorphism map separately. Lymphoid cells from two siblings with fucosidosis had 8-fold to 341-fold less intracellular α-l-fucosidase protein with 11-fold to 56-fold lower specific activities than control cells. Residual mutant enzyme was a glycoprotein with a polypeptide chain virtually the same size (M r=52,000) as control enzyme. However, residual mutant enzyme was hypoglycosylated and hypersecreted as compared to control enzyme.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00554076
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Biosynthesis, processing, and extracellular release of α-l-fucosidase in lymphoid cell lines of different genetic origins (1988)
    Springer
    Biochemical genetics 26 (1988), S. 401-420 
    Details
    ISSN: 1573-4927
    Keywords: α-l-fucosidase ; lymphoid cells ; fucosidosis ; serum polymorphism
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract In humans, the quantity of α-l-fucosidase in serum is determined by heredity. The mechanism controlling levels of the enzyme in serum is unknown. Lymphoid cell lines derived from individuals with either low, intermediate, or high α-l-fucosidase in serum were established. Steady-state levels of intracellular and extracellular α-l-fucosidase as well as rates of synthesis and secretion of enzyme overlapped among the cell lines. Thus,vivo} serum phenotypes were not expressed in this system. No appreciable differences in the qualitative processing of newly made α-l-fucosidase were observed among these lymphoid cell lines. Cells pulse-labeled with35S-methionine from 0.25 to 2 hr had an intracellular form of enzyme with aM r=58,000. Cells pulsed for 1.5 hr and chased for 21 hr with unlabeled methionine had an intracellular form ofM r=60,000 and an extracellular form ofM r=62,000. All three enzyme forms were glycoproteins with a common polypeptide chain ofM r=52,000 but with different carbohydrate moieties. No evidence for a high molecular mass precursor form of α-l-fucosidase was found. Fucosidosis is a rare, inherited disease in which α-l-fucosidase activity in tissues and body fluids is low or absent. The mutations for fucosidosis and the serum polymorphism map separately. Lymphoid cells from two siblings with fucosidosis had 8-fold to 341-fold less intracellular α-l-fucosidase protein with 11-fold to 56-fold lower specific activities than control cells. Residual mutant enzyme was a glycoprotein with a polypeptide chain virtually the same size (M r=52,000) as control enzyme. However, residual mutant enzyme was hypoglycosylated and hypersecreted as compared to control enzyme.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02401794
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
  • 4
    Electronic Resource
    Electronic Resource
    Specific activity of α-l-fucosidase in sera with phenotypes of either low, intermediate, or high total enzyme activity and in a fucosidosis serum (1986)
    Springer
    Biochemical genetics 24 (1986), S. 115-130 
    Details
    ISSN: 1573-4927
    Keywords: specific activity ; α-l-fucosidase ; serum polymorphism ; fucosidosis ; enzyme-linked immunoabsorbent assay (ELISA)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract The quantity of α-l-fucosidase activity in human serum is determined by heredity. An individual may inherit either low, intermediate, or high serum enzyme activity. An enzyme-linked immunoabsorbent assay has been developed that can detect 0.3 ng of α-l-fucosidase protein. Enzyme protein in serum of 102 individuals ranged from 20 to 835 ng/ml. The group included individuals with low, intermediate, and high enzyme activity. The specific activity of α-l-fucosidase within this group was statistically the same (mean±SD=11,002±1051 U/mg). Thus, individuals with low and intermediate enzyme activity in serum had lower amounts of enzyme protein with the same specific activity as in individuals with high enzyme activity. Fucosidosis is a rare inherited disease in which α-l-fucosidase activity in tissues and body fluids is low or absent. The concentrations of enzyme protein in sera of a fucosidosis patient and parents were 76, 565, and 604 ng/ml, respectively, and the specific activities of enzyme were 1316, 8938, and 8858 U/mg, respectively. Thus, the fucosidosis serum probably contained a structurally altered enzyme with reduced catalytic activity. The somewhat low specific activities in the parents suggested that their sera contained both structurally altered and normal protein.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00502983
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    Paper (German National Licenses)
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  • 5
    Electronic Resource
    Electronic Resource
    Mouse strain differences in operant self-administration of ethanol (1987)
    Springer
    Behavior genetics 17 (1987), S. 439-451 
    Details
    ISSN: 1573-3297
    Keywords: oral self-administration ; operant behavior ; C57BL/6J mice ; BALB/cJ mice ; alcohol ; behavior genetics
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Psychology
    Notes: Abstract By the use of operant conditioning procedures, we determined whether mice from two strains, C57BL/6J and BALB/cJ, differ in ethanol-reinforced behavior. To establish ethanol as a reinforcer, drinking was induced by feeding mice prior to the 30-min experimental session. Initially mice received water and then a series of increasing ethanol concentrations (1, 2, 4, and 8%, w/v) in response to a lever press. The volume of liquid consumed per unit of body weight remained relatively constant across concentrations, and thus the amount of ethanol consumed (g/kg) increased with increases in ethanol concentration. At all concentrations the C57BL/6J mice drank larger volumes than the BALB/cJ mice. After shifting the time of feeding from before to after the session, the consumption of 8% ethanol declined 56% for the C57B/6J mice and 81% for the BALB/cJ mice. To determine if ethanol was serving as a reinforcer, behavior and intake were then compared during ethanol and water availability. The ethanol consumption of the C57BL/6J mice markedly exceeded the water consumption and resulted in blood ethanol levels of 199 ±27 mg/dl. These levels significantly exceeded the 8% ethanol intake of the BALB/cJ mice, while 0% intake was low and not significantly different between strains. The 8% ethanol drinking of the BALB/cJ mice did not differ from their water drinking. Thus, ethanol was established as a positive reinforcer for C57BL/6J mice but not for BALB/cJ mice.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01073111
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    Paper (German National Licenses)
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