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  • Articles: DFG German National Licenses  (7)
  • Biochemistry and Biotechnology  (4)
  • Nonselective cationic current  (3)
  • 1
    Electronic Resource
    Electronic Resource
    Inhibitory effect of phorbol 12, 13 dibutyrate on carbachol-activated nonselective cationic current in guinea-pig gastric myocytes (1997)
    Springer
    Pflügers Archiv 434 (1997), S. 505-507 
    Details
    ISSN: 1432-2013
    Keywords: Key words Carbachol ; Nonselective cationic current ; Protein kinase C ; smooth muscle
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract  The effect of protein kinase C (PKC) on carbachol (CCh)-activated nonselective cationic current (I CCh) was investigated in guinea-pig gastric myocytes using a PKC activator, phorbol 12, 13 dibutyrate (PDBu). Pretreatment with 1 μ M PDBu suppressed I CCh by 96.5 ± 2.9% (n = 14) in a reversible manner in nystatin-perforated mode. In the presence of 1 μM chelerythrine , a PKC inhibitor, inhibition of I CChby PDBu was not seen. In whole-cell mode, the inhibition of I CCh by PDBu was dependent on intracellular MgATP. In the presence of MgATP in the pipette, PDBu decreased I CCh by 98.8 ± 1.2% (n = 5) as was observed in nystatin-perforated mode. However, PDBu had little effect on I CCh in the absence of MgATP in the pipette; the extent of inhibition was 12.7 ± 4.3% (n = 8). PDBu also suppressed the generation of cationic current induced by intracellularly perfused GTP[γS]. In the PDBu-pretreated group (n = 9) and PDBu-untreated control group (n = 6), GTP[γS]-induced currents were 6.7 ± 2.4 pA and 236 ± 23 pA, respectively. These results suggest that PKC modulates I CCh at postreceptor sites via protein phosphorylation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004240050429
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Effects of myosin light chain kinase inhibitors on carbachol-activated nonselective cationic current in guinea-pig gastric myocytes (1997)
    Springer
    Pflügers Archiv 434 (1997), S. 346-353 
    Details
    ISSN: 1432-2013
    Keywords: Key words Smooth muscle ; Nonselective cationic current ; Carbachol ; Myosin light chain kinase ; ML-7
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract  The effects of myosin light chain kinase inhibitors on muscarinic stimulation-activated nonselective cationic current (I CCh) in guinea-pig gastric antral myocytes were studied using the whole-cell patch-clamp technique. I CCh was induced by carbachol (CCh, 50 μM) at a holding potential of –30 mV or –60 mV. ML-7, a chemical inhibitor of myosin light chain kinase (MLCK), inhibited I CCh concentration dependently in a reversible manner (53 ± 8.6% at 1 μM, mean ± SE, n = 11). In addition, amplitudes of I CCh were only 37 ± 2.7% of the daily control values following the addition of a peptide inhibitor of MLCK to the pipette solution. On the other hand, ML-7 had an inhibitory effect on voltage-operated Ca2+ channel current. The peak value of Ba2+ current at 0 mV was reduced to 35 ± 7.4% (n = 9) by 3 μM of ML-7. As I CCh is known to have an intracellular Ca2+ dependence, we tried to exclude the possibility that ML-7 inhibited I CCh indirectly via suppression of Ca2+ current and the similar inhibitory effects of ML-7 on I CChwere confirmed under the following conditions: (1) clamp of membrane potential at –60 mV; (2) clamp of intracellular [Ca2+] to 1 μM by 10 mM BAPTA; (3) pre-inhibition of Ca2+ channel by verapamil. Different from the effects on I CCh, ML-7 barely inhibited the same cationic current induced by guanosine 5’-O-(3-thiotriphosphate) (GTP[γS], 0.2 mM) in the pipette solution. These results suggest that a Ca2+/calmodulin-MLCK-dependent pathway can modulate the activation of I CCh in guinea-pig gastric antral myocytes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004240050407
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  • 3
    Electronic Resource
    Electronic Resource
    Protein kinase C mediates the desensitization of CCh-activated nonselective cationic current in guinea-pig gastric myocytes (1998)
    Springer
    Pflügers Archiv 436 (1998), S. 1-8 
    Details
    ISSN: 1432-2013
    Keywords: Key words Smooth muscle ; Nonselective cationic current ; Carbachol (CCh) ; Protein kinase C (PKC) ; Desensitization
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract  The possibility of the protein kinase C (PKC) pathway being a mechanism underlying the desensitization of carbachol- (CCh-)activated nonselective cationic current (I CCh) was investigated in a study of guinea-pig gastric myocytes. Using the conventional whole-cell patch-clamp technique with symmetrical CsCl-rich solution in pipette and bath, I CCh was induced by bath application of 50 µM CCh. With 0.5 mM EGTA [ethyleneglycol-bis(β-aminoethyl ether)-N,N,N′,N′-tetraacetic acid] in the pipette solution (0.5 mM [EGTA]i), I CCh decayed spontaneously (desensitization of I CCh) to around 20% within 10 min. Desensitization of I CCh was significantly attenuated with 2 mM [EGTA]i. At a concentration of 20 µM OAG (1-oleoyl-2-acetyl-sn-glycerol), a PKC activator, inhibited I CCh at 0.5 mM [EGTA]i but far less at 2 mM [EGTA]i (18% and 81% of control, respectively). The same cationic current induced by intracellular guanosine-5′-O-(3-thiotriphosphate) (GTP[γ-S]) was not inhibited by OAG with 0.5 mM [EGTA]i. The pretreatment of gastric myocytes with PKC inhibitors, either 1 µM chelerythrine or 1 µM peptide inhibitor, attenuated the desensitization of I CCh. [Ca2+]i was also measured by single cell microfluorometry using fura-2. Under CCh stimulation with 2 mM [EGTA]i, [Ca2+]i did not increase above 100 nM while it increased to around 260 nM with 0.5 mM [EGTA]i. These results suggest that the desensitization of I CCh is partly due to the Ca2+-dependent PKC pathway in guinea-pig gastric myocytes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004240050597
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Some factors determining protein aggregation during ultrafiltration (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 42 (1993), S. 260-265 
    Details
    ISSN: 0006-3592
    Keywords: fouling ; ultrafiltration ; protein aggregates ; field emission scanning electron microscopy (FESEM) ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The factors contributing to protein aggregation in albumin ultrafiltration were investigated as a function of operation conditions. The nature of protein deposits was examined by electron microscopy. Protein aggregation appears to occur as a result of rapid supersaturation of protein molecules and high solvent velocity (shear) in the concentrated layer near the membrane surface. The shear occurring in the solvent flow on the membrane surface probably unfolds protein molecules and thus promotes flocculation due to collision between particles. © 1993 John Wiley & Sons, Inc.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260420216
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  • 5
    Electronic Resource
    Electronic Resource
    Effect of membrane morphology and operation on protein deposition in ultrafiltration membranes (1995)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 47 (1995), S. 174-180 
    Details
    ISSN: 0006-3592
    Keywords: ultrafiltration membranes ; protein fouling ; BET measurements ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Membrane morphology is compared to protein depostion under passive adsorption and ultrafiltration conditions. Solute resistance of protein deposits for membranes of varying roughness, structure, and permeability can vary dramatically with operating conditions. Using Brunauer-Emmett-Teller adsorption isotherm (BET), study of the internal area and accessibility of several uttrafiltration membranes to protein deposition allows better understanding of the fouling mechanisms and interpretation of adsorbed protein quantities. © 1995 John Wiley & Sons, Inc.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260470208
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  • 6
    Electronic Resource
    Electronic Resource
    Acid hydrolysis of sweet potato for ethanol production (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 27 (1985), S. 316-320 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Studies were conducted to establish optimal conditions for the acid hydrolysis of sweet potato for maximal ethanol yield. The starch contents of two sweet potato cultivars (Georgia Red and TG-4), based on fresh weight, were 21.1 ± 0.6% and 27.5 ± 1.6%, respectively. The results of acid hydrolysis experiments showed the following: (1) both hydrolysis rate and hydroxymethylfurfural (HMF) concentration were a function of HCL concentration, temperature, and time; (2) the reducing sugars were rapidly formed with elevated concentrations of HCl and temperature, but also destroyed quickly; and (3) HMF concentration increased significantly with the concentration of HCl, temperature, and hydrolysis time.Maximum reducing sugar value of 84.2 DE and 0.056% HMF (based on wet weight) was achieved after heating 8% SPS for 15 min in 1N HCl at 110°C. Degraded 8% SPS (1N HCl, 97°C for 20 min or 110°C for 10 min) was utilized as substrate for ethanol fermentation and 3.8% ethanol (v/v) was produced from 1400 mL fermented wort. This is equal to 41.6 g ethanol (200 proof) from 400 g of fresh sweet potato tuber (Georgia Red) or an ethanol yield potential of 431 gal of 200-proof ethanol/acre (from 500 bushel tubers/acre).
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260270316
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  • 7
    Electronic Resource
    Electronic Resource
    Acid hydrolysis of Jerusalem artichoke for ethanol fermentation (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 28 (1986), S. 138-141 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260280124
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