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  • 1985-1989  (8)
  • 1988  (8)
  • Cell & Developmental Biology  (3)
  • serum polymorphism  (2)
  • sodium taurocholate  (2)
  • BALB/cJ mice
Source
Material
Years
  • 1985-1989  (8)
Year
Keywords
  • 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)
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  • 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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  • 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
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Lack of linear correlation between hepatic ligand uptake rate and unbound ligand concentration does not necessarily imply receptor-mediated uptake (1988)
    Springer
    Journal of pharmacokinetics and pharmacodynamics 16 (1988), S. 397-411 
    Details
    ISSN: 1573-8744
    Keywords: hepatic uptake ; albumin receptor-mediated hepatic uptake ; sodium taurocholate ; plasma protein binding
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Previous studies of the hepatic uptake of several albumin-bound ligands, using constant and variable albumin concentrations, were interpreted as being inconsistent with the traditional mechanism of uptake, defined as an uptake rate directly proportional to unbound ligand concentration, and led to the formulation of the albumin receptor theory of hepatic uptake. Because other experimental designs have failed to confirm the albumin receptor theory, we reexamined, using the isolated perfused rat liver preparation, the traditional uptake mechanism under the conditions used in the original studies, of constant and variable albumin concentration. Livers (n=6) were perfused in randomized sequence with 10 different solutions containing 24-14C-taurocholate in a single-pass design. Five solutions contained fixed albumin (0.1 mM) and variable taurocholate (3–48 μM) concentrations, and five maintained the taurocholate-albumin ratio fixed at 0.06; absolute concentrations of taurocholate varied from 3–48 μM, and of albumin from 0.05–0.08 mM. At constant albumin concentration in hepatic inflow, elimination rate of taurocholate was linearly related to both total (Cin) and unbound (Cin,u) taurocholate concentration in hepatic inflow, indicating first-order elimination kinetics. When taurocholate and albumin were increased in hepatic inflow in a fixed molar ratio, taurocholate uptake rate was not linearly related to Cin,u but was still consistent with the traditional uptake mechanism. Moreover, the apparent saturation of taurocholate uptake by added albumin was consistent with the reduction in unbound fraction (fu) in accordance with the traditional uptake mechanism. This study shows that although the traditional uptake mechanism dictates that ligand uptake rate is linearly related to unbound ligand concentration within the liver, uptake rate need not necessarily be linearly related to Cin,u.. Therefore, experiments in which lack of a linear relationship between uptake rate and Cin,u is found do not necessarily imply receptor-mediated uptake.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01062553
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  • 5
    Electronic Resource
    Electronic Resource
    Effect of a protein binding change on unbound and total plasma concentrations for drugs of intermediate hepatic extraction (1988)
    Springer
    Journal of pharmacokinetics and pharmacodynamics 16 (1988), S. 529-542 
    Details
    ISSN: 1573-8744
    Keywords: plasma protein binding displacement ; unbound fraction ; unbound concentration ; intrinsic clearance ; sodium taurocholate ; sodium oleate ; isolated perfused rat liver
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract For substances eliminated from blood by the liver, the effect of a change in unbound fraction of drug (fu b )on steady state total (C b )and unbound (Cu b )blood concentrations has hitherto only been considered for the two limiting cases, i.e., at the upper and lower extremes of hepatic intrinsic clearance (CL int ).For a substance of very low CL int ,if fu b changes, C t will change and Cu b will remain constant, whereas if CL int isvery high, Cu b will change and C b will remain constant.The present study defines the effects of a change in fu b on C b and Cu b over the whole CL int range. Computer simulations were undertaken which predicted that, for a given change in fu b ,absolute and relative changes in C b would decreasenonlinearly with increasing CL int, twhile the relative change in Cu b would increasewith CL int .The absolute change in Cub would be independent of CL int .Significant changes in Cb and Cu b would be observed at intermediate values of CL int not just at the high and low extremes. These theoretical predictions were investigated experimentally in the isolated perfused rat liver by examining the effects of a change in fu b of sodium taurocholate a substance with intermediate CL int (such that at fu b =0.27,hepatic extraction ratio=0.71) induced by concurrent administration of sodium oleate. Sodium 24- 14 C-taurocholate (specific activity 52 μCi/mmol) was infused into the reservoir in a recycling system at 30 μmol/hr for 105 min (n=6). At 45 min a bolus dose of sodium oleate (50 mmol) was administered to the reservoir, followed by a constant infusion of 143 mmol/hr for 1 hr. Following the administration of oleate, taurocholate fu b fell promptly by 55% (0.27–0.12). There was a relative increase of taurocholate C b of 22.7% and a relative decrease in Cu b of 45.4%, in accordance with the simulations (p〈0.05). We conclude that important changes in unbound steady-state concentration, the pharmacologically active moiety, can occur upon changes in unbound fraction with compounds of intermediate hepatic intrinsic clearance.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01062383
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    Paper (German National Licenses)
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  • 6
    Electronic Resource
    Electronic Resource
    Tissue-specific analogues of erythrocyte protein 4.1 retain functional domains (1988)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 37 (1988), S. 269-284 
    Details
    ISSN: 0730-2312
    Keywords: membrane skeleton ; nonerythroid protein 4.1 homologues immunoreative isoforms ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Analogues of the human erythroid membrane skeletal component protein 4.1 have been identified in perfused rat tissues and human T and B lymphocyte cell lines, olyclonal antibodies were used which are specific for all domains of protein 4.1, the spectrin-actin-promoting 8-Kd peptide, the membrane-binding 30-Kd domain, and the 50-Kd domain. Antibody reactivity, by Western blotting of tissue homogenates, shows reactivity with proteins varying in molecular weight from 175 Kd to 30 Kd. Further, these protein 4.1 analogues appear to be expressed in a tissue-specific fashion. Of the analogues detected there appear to be at least three classes: analogues containing all erythroid protein 4.1 domains, analogues containing all domains but with modified antigenic epitopes, and analogues containing only some domains. Chemical cleavage at cysteine linkages indicates that in analogues containing the 30-Kd region the location of cysteine is highly conserved. This datum suggests that in nonerythroid 4.1 isoforms of higher molecular weight the additional protein mass is added to the amino terminal end (30 Kd end).
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240370303
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  • 7
    Electronic Resource
    Electronic Resource
    Nerve pathways between the pterygopalatine ganglion and eye in cats (1988)
    New York, NY [u.a.] : Wiley-Blackwell
    The @Anatomical Record 222 (1988), S. 95-102 
    Details
    ISSN: 0003-276X
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: By dissection of thiocholine-stained orbital preparations, it has been determined that three different nerve pathways link the pterygopalatine ganglion and the eye in cats. (1) Nerves from the proximal half of the ganglion join a plexus of nerves and ganglion cells in the rete mirabile of the maxillary artery. Branches of the internal carotid nerve also supply this plexus. Fine nerves from the plexus travel to the optic nerve and then to the eye, accompanying both the nasociliary nerve that passes through the rete and the ciliary arteries that arise from the rete. (2) One or more nerves from the nerve of the pterygoid canal and from a prominent accessory ganglion near the orbital apex course to the inferior optic nerve surface at the optic foramen; these then run distally along the optic nerve to fuse with ciliary nerves or to accompany ciliary arteries entering the eye. (3) Other nerves from the pterygopalatine ganglion travel medially around the extraocular muscle cone to join the ethmoidal and infratrochlear branches of the nasociliary nerve; some nerves from the ganglion then take a retrograde course to the optic nerve, where they join ciliary nerves or arteries to the eye. All three pathways may transmit sympathetic, parasympathetic and somatic sensory nerve fibers.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/ar.1092220114
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    Paper (German National Licenses)
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  • 8
    Electronic Resource
    Electronic Resource
    Principles of antibody catalysis (1988)
    New York, NY : Wiley-Blackwell
    BioEssays 9 (1988), S. 107-112 
    Details
    ISSN: 0265-9247
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Antibodies have now been shown to catalyze a variety of chemical transformations, including hydrolytic, concerted, and bimolecular reactions. The inherent chirality of the antibody binding pocket has been exploited to exert precise stereochemical control over their catalyzed reactions. The mechanisms by which antibodies catalyze reactions are not expected to differ in any general way from those of natural enzymes. Antibodies use their binding energy to stabilize species of higher free energy which appear along the reaction coordinate or effect general acid/base catalysis. The advent of catalytic antibodies promises new catalysts that extend the range of catalysis by proteins to chemical transformations that were not required during the evolution of enzymes.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bies.950090402
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