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  • ATPase  (1)
  • Carnegiea gigantea  (1)
  • Cell & Developmental Biology  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Use of saguaro fruit by white-winged doves: isotopic evidence of a tight ecological association (2000)
    Springer
    Oecologia 124 (2000), S. 536-543 
    Details
    ISSN: 1432-1939
    Keywords: Key words Saguaro ; Carnegiea gigantea ; Stable isotope ratios ; Resource use ; Zenaida asiatica mearnsii
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract  We report the use of stable isotope and crop content analyses to quantify the use of saguaro (Carnegiea gigantea) nectar and fruit by migratory desert white-winged doves (Zenaida asiatica mearsnii). Saguaro resources had characteristically 13C-enriched CAM values (δ13C=–12.8±0.7‰ SD VPDB and –13.1±0.5‰ SD VPDB for nectar and fruit, respectively) relative to other food plants used by doves (δ13CC3=–24.9±3.3‰ SD VPDB). The water contained in saguaro nectar and fruit was deuterium enriched (δD=19.6±2.0‰ SD VSMOW and 48.4±1.6‰ SD VSMOW for nectar and fruit, respectively) relative to other water sources (ranging from –41 to –19‰ VSMOW). During the fruiting season, there was a positive correlation between δ13C in dove liver tissues and percent of saguaro in crop contents. A two-point mixing model indicated that during the peak of saguaro fruit use, most of the carbon incorporated in dove tissues was from saguaro. Desert white-winged doves appear to be saguaro specialists. Averaged over the period when doves were resident, saguaro comprised about 60% of the total carbon incorporated into dove tissues. Tissue δ13C and δD of body water showed a significant positive correlation, indicating that doves were using saguaro as a source of both nutrients and water. However, at the peak of saguaro utilization, the doves’ body-water δD was more positive (by about 20‰) than saguaro fruit water. We hypothesize that this enrichment is due to fractionated evaporative water losses by doves. Using dove carbon isotope data and a two end-point mixing model we estimate that, on average, doves consume the equivalent of 128 saguaro fruits per season; each fruit contains on average 26.0±14.8 g SD of pulp (wet mass) of which 19.4 g is water. Stable isotopes have been used to produce qualitative re-constructions of animal diets. Our study shows that they can be used to provide quantitative estimates of the flow of nutrients from resources into consumers as well.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004420000406
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  • 2
    Electronic Resource
    Electronic Resource
    Isolation and characterization of P-type H+-ATPase genes from potato (1994)
    Springer
    Plant molecular biology 26 (1994), S. 979-988 
    Details
    ISSN: 1573-5028
    Keywords: ATPase ; phloem loading ; plasma membrane ; Solanum tuberosum L. ; multigene family ; sucrose transporter
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract H+-ATPase cDNAs were identified in a potato leaf library using an Arabidopsis gene as a probe. Based on their sequences, the clones could be grouped into at least two classes. A similar classification was obtained from the analysis of sequence data from four tobacco genes. Both potato genes are expressed in all tissues analysed, higher levels of expression were found in leaves and stem than in roots and tubers. For both genes, no significant differences in level of expression could be detected under a variety of conditions such as cold treatment, anaerobiosis, sucrose induction or treatment with a synthetic cytokinin. Only 2,4-D and prolonged periods of darkness lead to a slight reduction in mRNA levels. The reduction in darkness was compensated after transfer of the plants back into the light. Expression of the ATPase genes remained constant in transgenic plants which are inhibited in phloem loading due to antisense inhibition of the sucrose transporter. On the other hand, expression of the sucrose transporter is inducible by auxin and cytokinin but not by sucrose. Taken together, these data suggest that at least the two plasma membrane H+-ATPase genes analysed are rather constant in their expression and that either other genes respond to external stimuli or that most of the regulation occurs at the post-transcriptional level.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00028864
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  • 3
    Electronic Resource
    Electronic Resource
    Immunological approach to the characterization of the outer acrosomal membrane of boar spermatozoa (1985)
    New York, NY : Wiley-Blackwell
    Gamete Research 11 (1985), S. 143-155 
    Details
    ISSN: 0148-7280
    Keywords: spermatozoa ; acrosomal membrane ; membrane antigens ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Antiserum to purified boar spermatozoan outer acrosomal membrane (OAM) was raised in rabbits and adsorbed with boar liver and serum glutaraldehyde cross-linked immunoadsorbents. The IgG fraction of the antiserum was purified by (NH4)2SO4 precipitation followed by ion-exchange chromatography. Indirect immunofluorescence showed bright fluorescent staining of the acrosomal cap of boar spermatozoa and to a lesser extent of the acrosomes of bull and goat spermatozoa after incubation with anti-OAM-IgG. Immuno-electron microscopy further confirmed the specificity of the antibody for the OAM. Preincubation of the anti-OAM-IgG with isolated OAM, completely abolished its reactivity. When tested by ELISA, anti-OAM-IgG reacted with boar, bull, goat, and human spermatozoa; however, its binding activity to boar spermatozoa was significantly greater as compared to spermatozoa from the other species tested.In an effort to identify OAM antigens recognized by this antiserum, the isolated boar OAM was labeled either with 3H or with 125I and solubilized by mild detergent treatment. The extracted components were immunoprecipitated with anti-OAM-IgG and protein A-bearing S. aureus and the thus isolated antigens were analysed on SDS-PAGE. The results suggest that anti-OAM-IgG recognized one high molecular 3H-labeled glycoprotein (270 kd), and four 125I-labeled polypeptides of lower molecular weight of the boar OAM.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/mrd.1120110205
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