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  • 1
    Electronic Resource
    Electronic Resource
    Studien über Quercetin und seine Derivate (1893)
    Springer
    Monatshefte für Chemie 14 (1893), S. 53-55 
    Details
    ISSN: 1434-4475
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01517855
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  • 2
    Electronic Resource
    Electronic Resource
    Studien über Quercetin und seine Derivate (1893)
    Springer
    Monatshefte für Chemie 14 (1893), S. 39-52 
    Details
    ISSN: 1434-4475
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01517854
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Synthesis, saludiuretic, and antihypertensive activity of 6,7-disubstituted 1(2H)- and 3,4-dihydro-1(2H)-phthalazinones (1986)
    s.l. : American Chemical Society
    Journal of medicinal chemistry 29 (1986), S. 947-959 
    Details
    ISSN: 1520-4804
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/jm00156a011
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  • 4
    Electronic Resource
    Electronic Resource
    Flow of Suspensions through Porous Media—Application to Deep Filtration (1970)
    s.l. : American Chemical Society
    Industrial & engineering chemistry 62 (1970), S. 8-35 
    Details
    ISSN: 1520-5045
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/ie50725a003
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  • 5
    Electronic Resource
    Electronic Resource
    Beitrage zur chemie der silicium-stickstoff-verbindungen 87. Ein neues, unerwartetes Si,N,C-Spiran aus siliciumtetrachlorid undnatrium-bis(trimethylsilyl)amid
    Amsterdam : Elsevier
    Journal of Organometallic Chemistry 23 (1970), S. 373-384 
    Details
    ISSN: 0022-328X
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/S0022-328X(00)92950-4
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  • 6
    Electronic Resource
    Electronic Resource
    Opposite effects of angiotensin II and the protein kinase C activator OAG on cardiac Na+ channels (1992)
    Springer
    The journal of membrane biology 130 (1992), S. 183-190 
    Details
    ISSN: 1432-1424
    Keywords: Na+ channel properties ; protein kinase C ; angiotensin II ; OAG ; phosphorylation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary Elementary Na+ currents were recorded at 19°C in cell-attached and inside-out patch-clamp experiments to study the influence of the vasoactive peptide angiotensin II (A II) and of the diacylglycerol analogue OAG (1-oleoyl-2-acetyl-snglycerol) on open probability and gating properties of single cardiac Na+ channels from cultured neonatal rat cardiocytes. Treating the cardiocytes with A II caused Na+ channel activation: reconstructed peak INa increased to 137 ± 17.5% of control at 3 μmol/liters and to 176 ± 42% at 30 μmol/liter. This NPo increase developed without major changes in open state and burst activity, even at 30 μmol/liter. OAG (6 μmol/liter) did not mimic this A II action. By contrast, OAG treatment of the cardiocytes had the opposite effect on NPo and diminished reconstructed peak INa to 67 ± 4.9% of the control. The putative protein kinase C inhibitor staurosporine (0.2 μmol/liter) abolished this INa depression and led to a normalization of NPo. OAG had the same effect on isolated Na+ channels. Exposure of the cytoplasmic surface of inside-out patches to 1 μmol/liter OAG reversibly depressed, in the simultaneous presence of 50 μmol/liter Mg-ATP, the reconstructed peak INa to 40 ± 9.7% of the control but left i unit, τ open and burst activity unaffected. No NPo depression was obtained in the absence of Mg-ATP indicating that Mg-ATP may serve as phosphate donor. Obviously, after phosphorylation by protein kinase C, cardiac Na+ channels attain a reduced open probability but appear to preserve their kinetic properties. It is also concluded that activation of protein kinase C is not the mechanism underlying the A II induced channel activation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00231895
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  • 7
    Electronic Resource
    Electronic Resource
    Na+ channel blockade by cyclic AMP and other 6-aminopurines in neonatal rat heart (1991)
    Springer
    The journal of membrane biology 119 (1991), S. 163-170 
    Details
    ISSN: 1432-1424
    Keywords: single cardiac Na+ channels ; phosphorylation ; cAMP ; ATP ; adenine
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary Elementary Na+ currents were recorded at 19°C in cell attached and inside-out patches from cultured neonatal rat cardiocytes in order to study the effect of cAMP and other 6-aminopurines. The treatment of the cardiocytes with db-cAMP (1×10−3 mol/liter) led to a decline of reconstructed macroscopic peakI Na to 62±7.6% of the initial control value. This reduction in NP0 was mostly accompanied by a decrease in burst activity. Openstate kinetics were preserved even in DPI-modified, noninactivating Na+ channels. Since the stimulator of the adenylate cyclase, forskolin (1×10−6 mol/liter), evoked a similar pattern of response, the NP0 decrease can be considered as the functional correlate of Na+ channel phosphorylation brought about by cAMP-dependent protein kinase. As found in inside-out patches, cAMP (1×10−3 mol/liter) remained effective under cell-free conditions and reduced reconstructed macroscopic peakI NA to about 50% of the initial control value when the absence of Mg-ATP at the cytoplasmic membrane surface prevents phosphorylation reactions. A very similar response developed in the cytoplasmic presence of other 6-aminopurines including ATP (1×103 mol/liter), adenosine (1×10−4 mol/liter), adenine (1×10−5 mol/liter) and hypoxanthine (1×10−5 mol/liter). This susceptibility to adenine suggests that cardiac Na+ channelsin situ could sense intracellular fluctuations of adenine nucleotides, most likely of ATP.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01871415
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  • 8
    Electronic Resource
    Electronic Resource
    Modification of single cardiac Na+ channels by DPI 201-106 (1986)
    Springer
    The journal of membrane biology 89 (1986), S. 163-172 
    Details
    ISSN: 1432-1424
    Keywords: inside-out patch clamp ; kinetic behavior of cardiac Na+ channels ; chemically eliminated inactivation ; piperazine indole ; isolated heart cells
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary In inside-out patches from cultured neonatal rat heart cells, single Na+ channel currents were analyzed under the influence of the cardiotonic compound DPI 201-106 (DPI), a putative novel channel modifier. In absence of DPI, normal cardiac single Na+ channels studied at −30 mV have one open state which is rapidly left with a rate constant of 826.5 sec−1 at 20°C during sustained depolarization., Reconstructed macroscopic currents relax completely with 7 to 10 msec. The current decay fits a single exponential. A considerable percentage of openings may occur during relaxation of the macroscopic current. In patches treated with 3×10−6 m DPI in the pipette solution, stepping to −30 mV results in drastically prolonged and usually repetitive openings. This channel activity mostly persists over the whole depolarization (usually 160 msec in duration) but is abruptly terminated on clamping back the patch to the holding potential. Besides these modified events, apparently normal openings occur. The open time distribution of DPI-treated Na+ channels is the sum of two exponentials characterized by time constants of 0.85 msec (which is close to the time constant found in the control patches, 1.21 msec) and 12 msec. Moreover, DPI-modified Na+ channels exhibit a sustained high, time-independent open probability. Similar to normal Na+ channels, the mean number of open DPI-modified Na+ channels is voltage-dependent and increases on shifting the holding potential in the hyperpolarizing direction. These kinetic changes suggest an elimination of Na+ channel inactivation as it may follow from an interaction of DPI with Na+ channels.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01869712
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  • 9
    Electronic Resource
    Electronic Resource
    Cyclic AMP inhibits contractility of detergent treated glycerol extracted cardiac muscle (1981)
    Springer
    Pflügers Archiv 391 (1981), S. 208-212 
    Details
    ISSN: 1432-2013
    Keywords: Myocardial contractility ; Troponin phosphorylation ; c-AMP ; Calcium ions ; Myocardial skinned fibres
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Glycerinated myocardial fibres treated with a detergent (Lubrol WX) and suspended in ATP salt solution produce half maximum isometric tension at pCa 6.2 (at pH 6.7). After addition of cyclic AMP (1–100 μM), the pCa required for half maximum activation is 5.9. c-AMP in concentrations of 1–100 μM induces a dose dependent inhibition (up to 40$ at pCa 6), and this effect can be amplified by the phosphodiesterase inhibitor IBMX (3-isobutyl-1-methylxanthine) 10−4 M. The effect is similar in presence and absence of sodium fluoride 10 mM. Since in detergent treated skinned fibres the cell membrane and the sarcoplasmic reticulum are extracted and since the Ca2+ ion concentration was kept constant and buffered, we propose that c-AMP does not act via the cell membrane or the sarcoplasmic reticulum, but via phosphorylation of troponin I. The latter is the only component which becomes phosphorylated in skinned fibres during c-AMP induced relaxation, an effect which is also responsible for the inhibition of actomyosin ATPase at constant Ca2+ ion concentration (cf. Ray and England 1976).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00596172
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  • 10
    Electronic Resource
    Electronic Resource
    Dependence of force and immediate stiffness on sarcomere length and Ca2+ activation in frog skinned muscle fibres (1981)
    Springer
    Pflügers Archiv 389 (1981), S. 97-103 
    Details
    ISSN: 1432-2013
    Keywords: Skinned muscle fibres, calcium activation of ; Skinned muscle fibres, effect of Mg-ATP ; Muscle stiffness, sarcomere length dependence ; Muscle force ; sarcomere length dependence
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract 1. Skinned fibres prepared from semitendinosus muscle of the frog (Rana temporaria) by a modified Natori's method were suspended in ATP-salt solution (pCa 5, pH 6.7, 3°C). Isometric tension was studied as a function of sarcomere length (determined by laser diffraction) and stiffness was measured by recording tension changes in response to quick changes in length performed within 0.5 ms during Ca2+ activated contractions. 2. There was a sigmoidal relationship between contractile tension or stiffness and pCa. The threshold Ca ion concentration was 5×10−7 M at a sarcomere length of 2.2 μm and a little lower at larger sarcomere lengths (as also described by Endo 1972). At all sarcomere lengths peak tension was reached at about 10−5 M Ca2+. 3. The skinned fibres produced maximum tension at sarcomere lengths of 2.0–2.3 μm. With a further increase in sarcomere length, contractile tension decreased. The relation between tension and sarcomere length was linear up to 3.2 μm above which value the relationship ‘tailed’. 4. Quick releases in the range of 0.1–0.5%L 0 applied during Ca2+ activation produced an immediate elastic fall in tension in phase with the length change followed by a quick recovery phase completed within about 10 ms. Conversely, a quick stretch produced an elastic increase followed by a rapid tension decay completed within about 8–10 ms. When the extreme tensions obtained during the length step were plotted versus the size of the length step, a force-extension diagram was obtained corresponding to the T1-curve of Huxley and Simmons (1973) which intercepted the length axis at about −8 nm/half sarcomere at all sarcomere lengths investigated. The slope of the linear portion of the T1-curve was taken to determine immediate stiffness which was proportional to tension when either sarcomere length or Ca2+ ion concentration were varied. 5. In conclusion tension and immediated stiffness are proportional to the extent of actin myosin filament overlap and hence to the number of possible crossbridges between thick and thin filaments. 6. At very low calcium ion concentrations (10−7 M) skinned fibres develop tension and become stiff when the Mg-ATP concentration is lowered (at constant [ATP] total) to values below 10−5 M. Under these conditions a quick release causes a drop in tension which is—as in the case of rigor—not followed by a fast recovery of tension. Again stiffness was independent of the direction and amplitude of quick length changes; but — as in the case of rigor — the stiffness to tension ratio was much higher than in Ca2+ activated contraction.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00582098
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