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  • 1
    Electronic Resource
    Electronic Resource
    Instrumental analysis of ethanol-induced intoxication in human males (1986)
    Springer
    Psychopharmacology 89 (1986), S. 8-13 
    Details
    ISSN: 1432-2072
    Keywords: Ethanol ; Blood ethanol concentration ; Instrumental response ; Verbal behavior ; Time-effect relations ; Human subjects
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract A study was conducted to assess subjective reports of intoxication during the ascending phase of the plasma ethanol curve. Eighteen male social drinkers were divided into three groups and were given either placebo, 0.347 g/kg ethanol or 0.694 g/kg ethanol under double-blind conditions. Subjects reported levels of intoxication both instrumentally, by moving a joystick device, and verbally using an 11-point self-rating scale. Compared to placebo, ethanol produced significantly higher verbal self-rating scores, but there were no differences in the scores between the low-and high-dose ethanol groups. Instrumental responses of ethanol effects did, however, distinguish between the two ethanol treatments. All subjects who received ethanol reliably detected its effects when plasma ethanol levels reached 32 mg/dl, but only the subjects who received the high dose reported episodes of intense well-being or euphoria. Ethanol-induced euphoria occurred while plasma ethanol levels were rapidly rising, and was characterized by multiple, paroxysmal episodes that typically lasted about 3 min each. This study demonstrated that a continuously available instrumental response provided sensitive and reliable measures of rapidly changing behavioral states associated with ethanol-induced intoxication.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00175181
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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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    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
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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
    Mathematical and mechanical modeling of heat transport through the heart (1987)
    Springer
    Annals of biomedical engineering 15 (1987), S. 603-617 
    Details
    ISSN: 1573-9686
    Keywords: Blood temperature ; Thermodilution ; Heat transport ; Cardiac output
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine , Technology
    Notes: Abstract Pulmonary artery blood temperature manifests large variations which obscure the measurement of cardiac parameters by thermodilution techniques. We have created three mathematical models of heat flow through the heart in order to better understand the origins of the temperature fluctuations in the pulmonary artery. These lumped parameter models are based on a serial connection of two mixing chambers, which correspond to the atrium and ventricle of the heart. We have used the models to predict temperature fluctuations in the outlet, based on measurements of inlet flow, inlet temperature, and the timing of the cardiac cycle, of a mechanical right artificial heart in a mock circulatory loop. The most complex model accurately predicts the outflow temperature from the input variables and provides a quantitative description of heat transport across the heart under many operating conditions. The simplified models illustrate the conditions under which is possible to predict the outflow temperature from the inflow temperatures alone.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02364252
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    Paper (German National Licenses)
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  • 6
    Electronic Resource
    Electronic Resource
    Signal processing strategies for enhancement of signal-to-noise ratio of thermodilution measurements (1988)
    Springer
    Annals of biomedical engineering 16 (1988), S. 265-278 
    Details
    ISSN: 1573-9686
    Keywords: Thermodilution ; Pulmonary artery blood temperature ; Signal processing ; Cardiac output
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine , Technology
    Notes: Abstract Thermodilution measurements of clinically important cardiac parameters, such as cardiac output and stroke volume, are subject to many sources of error. The temperature fluctuations (thermal noise) normally found in the pulmonary artery constitute one of these sources of errors. To improve the signal-to-noise ratio of thermodilution flow measurements rather than increase the signal level, we investigated four signal processing strategies designed to reduce the thermal noise power. We applied the noise reduction strategies to thermal noise data, containing simulated thermodilution curves, obtained in a mock circulatory loop. We compared the accuracy and reproducibility of the curve area estimates produced by the algorithms to the area estimates obtained by numerical integration of the thermal signal. Our results show that a bandpass (BP) integration technique combined with a noise canceler can improve thermodilution curve area estimate reproducibility and accuracy. The BP integration technique improved the reproducibility of cardiac output measurements by roughly 16 dB and is directly applicable to most thermodilution hardware currently in use. The more accurate noise cancelers, combined with the BP integration technique, provided correspondingly improved signal-to-noise ratios, with the improvement ranging up to 50 dB.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02368003
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    Paper (German National Licenses)
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