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  • 1
    Publication Date: 2012-12-21
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
    Publication Date: 2023-05-12
    Keywords: Akademik Nikolaj Strakhov; ANS4; ANS4-4502A; ANS4-4502B; ANS4-4504; ANS4-4507; ANS4-4508; ANS4-4510A; ANS4-4510B; ANS4-4512; ANS4-4516A; ANS4-4516B; ANS4-4518; ANS4-4519; ANS4-4531TG; Archive of Ocean Data; ARCOD; Bottom water temperature; Caribbean Sea; Conductivity, thermal; Elevation of event; Event label; Heat flow; Latitude of event; Longitude of event; MULT; Multiple investigations; Penetration depth; Temperature, in rock/sediment; Temperature (thermal) gradient; Thermometer
    Type: Dataset
    Format: text/tab-separated-values, 73 data points
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  • 3
    Publication Date: 2023-05-12
    Keywords: Akademik Nikolaj Strakhov; ANS4; ANS4-4401; ANS4-4402; ANS4-4404A; ANS4-4404B; ANS4-4404C; ANS4-4410A; ANS4-4410B; ANS4-4410C; ANS4-4411; ANS4-4413A; ANS4-4413B; ANS4-4413C; ANS4-4414; ANS4-4416TG; ANS4-4417; ANS4-4418; ANS4-4420; ANS4-4421; Archive of Ocean Data; ARCOD; Bottom water temperature; Conductivity, thermal; Elevation of event; Event label; Gulf of Mexico; Heat flow; Latitude of event; Longitude of event; MULT; Multiple investigations; Penetration depth; Temperature, in rock/sediment; Temperature (thermal) gradient; Thermometer
    Type: Dataset
    Format: text/tab-separated-values, 103 data points
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  • 4
    Publication Date: 2023-05-12
    Keywords: Area/locality; Conductivity, average; Depth, bottom/max; ELEVATION; Heat flow; LATITUDE; LONGITUDE; Method comment; Number; Number of temperature data; Sample, optional label/labor no; Temperature gradient
    Type: Dataset
    Format: text/tab-separated-values, 273 data points
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  • 5
    ISSN: 1432-1793
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We examined the relation of RNA/DNA ratios to growth for three size groups of the tropical scallop Euvola ziczac maintained in suspended culture at 8, 21 and 34 m in depth in the Golfo de Cariaco, Venezuel. Various growth parameters indicated that production decreased with depth. This was more likely due to a decrease in seston quality with depth than to temperatures or seston abundance (which were similar at the various depths studied). The RNA/DNA ratio was correlated with the G-index of muscle growth for juveniles (r 2=0.55). A much weaker correlation was observed for the maturing scallops (r 2=0.18), probably because of the interaction between reproductive and somatic growth. In fully mature scallops, somatic growth was negligible and the RNA/DNA ratios appeared to be inversely related to the level of physiological stress of the scallops. Whereas RNA/DNA ratios are difficult to interpret for maturing E. ziczac, because an increased ratio can be due to either increased gonadal or somatic growth, they are useful in predicting growth in juveniles and physiological stress in fully mature scallops.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Springer
    The journal of membrane biology 143 (1995), S. 227-235 
    ISSN: 1432-1424
    Keywords: Bicarbonate secretion ; Cl−/HCO 3 − exchange ; SITS ; Stationary microperfusion
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Secretion of bicarbonate has been described for distal nephron epithelium and attributed to apical Cl−/HCO 3 − exchange in beta-intercalated cells. We investigated the presence of this mechanism in cortical distal tubules by perfusing these segments with acid (pH 6) 10 mm phosphate Ringer. The kinetics of luminal alkalinization was studied in stationary microperfusion experiments by double-barreled pH (ion-exchange resin)/1 m KCl reference microelectrodes. Luminal alkalinization may be due to influx (into the lumen) of HCO 3 − or OH−, or efflux of H+. The magnitude of the Cl−/ HCO 3 − exchange component was measured by perfusing the lumen with solutions with or without chloride, which was substituted by gluconate. This component was not different from zero in control and alkalotic (chronic plus acute) Wistar rats. Homozygous Brattleboro rats (BRB), genetically devoid of antidiuretic hormone, were used since this hormone has been shown to stimulate H+ secretion, which could mask bicarbonate secretion. In these rats, no evidence for Cl−/HCO 3 − exchange was found in control BRB and in early distal segments of alkalotic animals, but in late distal tubule a significant component of 0.14±0.033 nmol/cm2 · sec was observed, which, however, is small when compared to the reabsorptive flow found in control Wistar rats, of 0.95±0.10 nmol/cm2 · sec. In addition, 5×10−4 m SITS had no effect on distal bicarbonate reabsorption in controls as well as on secretion in alkalotic Wistar and Brattleboro rats, which is compatible with the absence of effect of this drug on the apical Cl−/HCO 3 − exchange in other tissues. It is concluded that most distal alkalinization is not Cl− dependent, and that Cl−/HCO 3 − exchange may be found in cortical distal tubule, but its magnitude is, even in alkalosis, markedly smaller than the reabsorptive flux, which predominates in the rats studied in this paper, keeping luminal pH lower than that of blood.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    The journal of membrane biology 163 (1998), S. 137-145 
    ISSN: 1432-1424
    Keywords: Key words: MDCK cells — H+ ATPase — H+–K+ ATPase — Intracellular pH — Chloride
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract. MDCK cells display several acid-base transport systems found in intercalated cells, such as Na+-H+ exchange, H+–K+ ATPase and Cl−/HCO− 3 exchange. In this work we studied the functional activity of a vacuolar H+-ATPase in MDCK cells and its chloride dependence. We measured intracellular pH (pHi) in monolayers grown on glass cover slips utilizing the pH sensitive probe BCECF. To analyze the functional activity of the H+ transporters we observed the intracellular alkalinization in response to an acute acid load due to a 20 mm NH+ 4 pulse, and calculated the initial rate of pHi recovery (dpHi/dt). The cells have a basal pHi of 7.17 ± 0.01 (n= 23) and control dpHi/dt of 0.121 ± 0.006 (n= 23) pHi units/min. This pHi recovery rate is markedly decreased when Na+ was removed, to 0.069 ± 0.004 (n= 16). It was further reduced to 0.042 ± 0.005 (n= 12) when concanamycin 4.6 × 10−8 m (a specific inhibitor of the vacuolar H+-ATPase) was added to the zero Na+ solution. When using a solution with zero Na+, low K+ (0.5 mm) plus concanamycin, pHi recovery fell again, significantly, to 0.023 ± 0.006 (n= 14) as expected in the presence of a H+–K+-ATPase. This result was confirmed by the use of 5 × 10−5 m Schering 28080. The Na+ independent pHi recovery was significantly reduced from 0.069 ± 0.004 to 0.042 ± 0.004 (n= 12) when NPPB 10−5 m (a specific blocker of Cl− channels in renal tubules) was utilized. When the cells were preincubated in 0 Cl−/normal Na+ solution for 8 min. before the ammonium pulse, the pHi recovery fell from 0.069 ± 0.004 to 0.041 ± 0.007 (n= 12) in a Na+ and Cl− free solution. From these results we conclude that: (i) MDCK cells have two Na+-independent mechanisms of pHi recovery, a concanamycin sensitive H+-ATPase and a K+ dependent, Schering 28080 sensitive H+–K+ ATPase; and, (ii) pHi recovery in Na+-free medium depends on the presence of a chloride current which can be blocked by NPPB and impaired by preincubation in Cl−–free medium. This finding supports a role for chloride in the function of the H+ ATPase, which might be electrical shunting or a biochemical interaction.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Springer
    The journal of membrane biology 157 (1997), S. 193 -201 
    ISSN: 1432-1424
    Keywords: Key words: H+-ATPase — Transepithelial PD — Distal tubule — Bicarbonate reabsorption
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract. The presence of an electrogenic H+-ATPase has been described in the late distal tubule, a segment which contains intercalated cells. The present paper studies the electrogenicity of this transport mechanism, which has been demonstrated in turtle bladder and in cortical collecting duct. Transepithelial PD (V t ) was measured by means of Ling-Gerard microelectrodes in late distal tubule of rat renal cortex during in vivo microperfusion. The tubules were perfused with electrolyte solutions to which 2 × 10−7 m bafilomycin or 4.6 × 10−8 m concanamycin were added. No significant increase in lumen-negative V t upon perfusion with these inhibitors as compared to control, was observed as well as when 10−3 m amiloride, 10−5 m benzamil or 3 mm Ba2+ were perfused alone or in combination. The effect of an inhibition of electrogenic H+ secretion, i.e., increase in lumen-negative V t by 2–4 mV, was observed only when Cl− channels were blocked by 10−5 m 5-nitro-2-(3-phenylpropylamino) benzoic acid (NPPB). This blocker also reduced the rate of bicarbonate reabsorption in this segment from 1.21 ± 0.14 (n= 8) to 0.62 ± 0.03 (8) nmol.cm−2.sec−1 as determined by stationary microperfusion and pH measurement by ion-exchange resin microelectrodes. These results indicate that: (i) the participation of the vacuolar H+ ATPase in the establishment of cortical late distal tubule V t is minor in physiological conditions, but can be demonstrated after blocking Cl− channels, thus suggesting a shunting effect of this anion; and, (ii) the rate of H+ secretion in this segment is reduced by a Cl− channel blocker, supporting coupling of H+-ATPase with Cl− transport.
    Type of Medium: Electronic Resource
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  • 9
    ISSN: 1432-072X
    Keywords: Catabolic repression ; D-Xylose ; Hexokinase ; Invertase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The relationship between the xylose induced decrease in hexokinase PII activity and the derepression of invertase synthesis in yeast is described. When xylose was added to cells growing in a chemostat under nitrogen limitation, the catabolic repression was supressed as shown by the large increase on invertase levels even if glucose remained high. The glucose phosphorylating-enzymes were separated by hydroxylapatite chromatography and it is shown that the treatment with xylose is accompanied by a loss of 98% hexokinase PII and a 50% of the PI isoenzyme, whereas the levels of glucokinase as well as those of glucose-6-phosphate, fructose-6-phosphate, pyruvate and ATP remained unaffected. The analysis of the enzymes present in cells grown in ethanol, limiting glucose and high glucose, shows that hexokinase PII predominates in cells under catabolic repression, the opposite is true for glucokinase, whereas hexokinase PI remains unaffected.
    Type of Medium: Electronic Resource
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  • 10
    ISSN: 1432-072X
    Keywords: Isocitrate lyase ; Induction ; Catabolite repression ; Catabolite inactivation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The synthesis of isocitrate lyase was induced by the presence of ethanol in the chemostat reaching a specific activity of 200 mU·mg-1 at this induced state. In glucoselimited, derepressed cells, 20 mU·mg-1 were detected and under repressed conditions isocitrate lyase activity was not detected. The sensitivity of gluconeogenic enzymes: cytoplasmic malate dehydrogenase; fructose 1,6-bisphosphatase and isocitrate lyase as well as the mitochondrial enzymes NADH dehydrogenase and succinate cytochrome c oxidase to glucose and galactose repression were studied in chemostat cultures. Our results show that galactose was less effective as a repressor than glucose. Malate dehydrogenase was completely inactivated by glucose, whereas galactose only produced a 78% decrease of specific activity. Fructose 1,6-bisphosphatase and isocitrate lyase were completely inactivated by both sugars but at different rate. Glucose produced an 85% decrease of specific activity of the mitochondrial enzymes whereas galactose only decrease an 67%.
    Type of Medium: Electronic Resource
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