ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

feed icon rss

Your email was sent successfully. Check your inbox.

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

Proceed reservation?

Export
Filter
  • etintidine  (2)
  • Bovine somatotropin  (1)
  • Chondrichthyes
  • Freshwater adaptation
  • Growth rate
  • cardiomyocytes
  • Springer  (5)
  • 1995-1999  (2)
  • 1985-1989  (3)
Collection
Keywords
Publisher
  • Springer  (5)
Years
Year
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Molecular and cellular biochemistry 145 (1995), S. 131-139 
    ISSN: 1573-4919
    Keywords: glycogen phosphorylase ; alloxan-diabetes ; cardiomyocytes ; cGMP ; phosphodiesterase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract The focus of this study was to identify the molecular basis for the hypersensitive response of glycogen phosphorylase activation to epinephrine stimulation in alloxan diabetic-derived cardiomyocytes. Cyclic AMP levels were found not to be significantly different between normal and diabetic-derived cells while cGMP concentrations were found consistently to be significantly lower in diabetic-derived cells than in normal cells. Treatment with cyclic GMP analogues did not affect phosphorylase activation by epinephrine in normal cardiomyocytes whereas, IBMX, a nonselective phosphodiesterase inhibitor, had a significant effect on basal and agonist-stimulated phosphorylase activity in both normal and diabetic-derived cardiomyocytes. Differences in the time course for the rate of decay of phosphorylasea from agonist-stimulated to basal levels were observed between normal and diabetic cells. After 3 h in primary culture, phosphorylasea activity returned to basal levels more quickly in normal than in diabetic-derived cells while after 24 h in culture, the time for phosphorylasea decay was not significantly different between normal and diabetic myocytes and was longer than the 3 h response. After 3 h in primary culture, no significant difference in phosphorylase kinase activity was observed between normal and diabetic-derived cells exposed to epinephrine whereas, after 24 h in culture, phosphorylase kinase activity was significantly decreased in diabetic cells under basal and agonist-stimulated conditions. These data collectively suggest that the hypersensitive response of glycogen phosphorylase to epinephrine stimulation in diabetic-derived cardiomyocytes is not due to a defect present at the level of phosphorylase kinase but may, in part, result from an alteration in cardiac phosphodiesterase activity resulting from diminished intracellular cyclic GMP concentrations.
    Type of Medium: Electronic Resource
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 2
    Electronic Resource
    Electronic Resource
    Springer
    The protein journal 14 (1995), S. 559-566 
    ISSN: 1573-4943
    Keywords: Bovine somatotropin ; methemerythrin ; cytochrome b-562 ; cytochrome c′ ; CHARMM ; GROMOS ; UHBD
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Molecular dynamics simulations and energy analysis have been carried out to study the structural mobility and stability of the four α-helix bundle motifs. The simulation results as well as the X-ray data show that the atomic RMS fluctuation is larger at the loop region for four representative proteins investigated: methemerythrin, cytochrome b-562, cytochrome c′, and bovine somatotropin. The loop-loop, helix-helix, and loop-helix interactions are computed for the unfolded and folded proteins. In the folded and solvated protein structures the loop-helix interaction is stronger than the helix-helix interaction, especially in the electrostatic component. But the stabilization energies of both the loop-helix and the helix-helix interactions relative to the those of an unfolded structure are of the same order of magnitude. The stabilization due to protein-solvent interaction is greater in the helix region than in the loop region. The percentage of hydrophilic solvent accessible area for the four proteins studied was calculated with the method of Eisenberg and McLachlan. The percentage of the hydrophilic area is greater in the loops than in the helices. A Poisson-Boltzmann calculation shows that the potential from the loops acting on a helix is generally more negative than that from other helices.
    Type of Medium: Electronic Resource
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Journal of pharmacokinetics and pharmacodynamics 15 (1987), S. 557-568 
    ISSN: 1573-8744
    Keywords: etintidine ; propranolol ; 4-hydroxypropranolol ; interaction ; pharmacokinetics
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Etintidine HCl is a potent H2 -blocker. The effect of clinical doses of etintidine on the disposition of a single oral dose of propranolol was investigated in 12 normal subjects. This was a double-blind, two-way crossover study. Each subject received etintidine (400 mg) or placebo twice a day with meals for 4 days on two occasions (separated by 4 days). On each occasion, the subjects were fasted overnight on Day 3 and were given an oral dose of Inderal® (40 mg propranolol hydrochloride) 30 min following the administration of the morning dose of etintidine or placebo on Day 4. Blood samples were collected prior to and up to 24 hr following the administration of propranolol. The plasma samples were analyzed for propranolol and 4-hydroxypropranolol by HPLC. Comparison of the pharmacokinetic parameters of propranolol between etintidine and the placebo groups indicates that etintidine significantly increased the AUC0−∞,values (573.5 vs. 146.4 ng·hr/ml, p=0.0001)and prolonged the elimination half-life (4.61 vs. 2.33 hr) of propranolol. Statistical evaluation of the pharmacokinetic parameters of 4-hydroxypropanolol indicates that etintidine also increased the AUC0−24 values (43.8 vs. 16.4 ng·hr/ml, p=0.0028) and prolonged the elimination half-life (4.87 vs. 1.97 hr) of 4-hydroxypropranolol. The data suggest that etintidine, like cimetidine, impaired the elimination of propranolol. Etintidine also protracted the elimination of 4-hydroxypropranolol, an active metabolite of propranolol.
    Type of Medium: Electronic Resource
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 4
    ISSN: 1573-904X
    Keywords: etintidine ; high-performance liquid chromatography (HPLC) ; solid extraction ; determination of etintidine in plasma
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract This paper describes a new, rapid solid extraction method for the determination of etintidine in plasma. The method employs a semiautomatic sample preparation system. Plasma samples and the internal standard (cimetidine) were applied onto octyl-bonded silica extraction columns. The extraction columns were then subjected to Tris buffer and water wash and were subsequently loaded onto an automatic sample injection system. The contents of the extraction columns were eluted on-line with a mobile phase of acetonitrile:methanol:0.1% ammonium hydroxide (85:10:5, by volume) onto a silica analytical column and detected by UV absorption at 229 nm. The chromatographic condition separates etintidine from some of its metabolites and other endogenous components in plasma. The detection limit for etintidine was 0.02–0.05 µg/ml when 0.2 ml of plasma was used. This method has been used for the determination of plasma etintidine levels in humans and mice after oral administration of etintidine and was found to be suitable for pharmacokinetic/bioavailability studies of etintidine in humans and animals. The method can also be used for the quantitative determination of cimetidine and certain metabolites of etintidine.
    Type of Medium: Electronic Resource
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 5
    ISSN: 1573-5133
    Keywords: Batoidea ; Chondrichthyes ; Elasmobranchii ; Amazon ; Magdalena ; Maracaibo ; Orinoco ; Paraná-Paraguay
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Synopsis The number of venomous caudal spines and their length and position relative to one another were determined in seven species of South American freshwater rays (Potamotrygonidae) and eight marine or euryhaline species of four families from the Caribbean Coast of South and Central America. Most species have two visible spines at certain stages in the shedding-replacement cycle and only one visible spine at other stages (following shedding). If we include the embryological beginnings of the spines before they erupt and become visible, the spine counts of most rays are actually 2 rather than 1 or 2. Since most species apparently follow this pattern, spine counts are of little use in distinguishing between species except in the relatively few that may have only one, or no spines. Eight captive Potamotrygon specimens maintained in simulated tropical temperature conditions over 12 months showed periodic shedding and replacement of spines. The molts were biannual for a given ray but annual for a given spine. They alternated between two spine loci and their cycles were approximately six months out of phase with each other. Recent studies on Dasyatis sabina by others report only one molt per year, with replacement spines forming always posterior to the primary spine rather than alternating between posterior and anterior. Supernumerary spines (counts of more than two, up to five) are also discussed, as are counts of one and zero.
    Type of Medium: Electronic Resource
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...