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  • Articles  (56)
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  • 1
    Electronic Resource
    Electronic Resource
    Histochemical studies on the hyaline capsule of Holopedium gibberum Zaddach (Crustacea, Cladocera) (1970)
    Springer
    Histochemistry and cell biology 21 (1970), S. 160-169 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The jelly capsule of the “water flea” Holopedium gibberum, was subjected to histochemical procedures for the visualization of acid mucopolysaccharides, amino acids, and proteins. The affinity of the capsule for azure A, alcian blue, colloidal iron, aldehyde fuchsin, and iron diamine reagents, at low pH, indicates the presence of a sulfated mucopolysaccharide. The presence of carboxyl groups, in addition, is indicated by alcian blue affinity in the combined aldehyde fuchsin-alcian blue and high-iron diamine-alcian blue procedures, as well as by the restoration of weak, but definite, basophilia after methylation-saponification pretreatment. The capsule remained alcianophilic in solutions of MgCl2 as high as 0.4 molar. Cetylpyridinium blockade was removed by KCl solutions of 0.5–1.0 molar. The periodic acid-Schiff reaction was nil to very weak, in spite of extended oxidizing periods. None of the methods used for the visualization of amino acids or proteins gave unequivocally positive results. A possible origin of the capsular material is proposed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00306183
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  • 2
    Electronic Resource
    Electronic Resource
    Spatial variation in larval concentrations as a cause of spatial variation in settlement for the barnacle, Balanus glandula (1985)
    Springer
    Oecologia 67 (1985), S. 267-272 
    Details
    ISSN: 1432-1939
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Settlement rates of the high intertidal barnacle, Balanus glandula, were monitored at three sites in the rocky intertidal zone in Central California simultaneously with measurements of larval concentrations in the adjacent water column. In both 1983 and 1984, settlement rates onto vacant substrate differed among the sites by nearly two orders of magnitude. For all sampling dates, this spatial variation in settlement mirrored the spatial distribution of Balanus glandula cyprid concentration in the water column. A perfect rank correlation was found between cyprid concentrations near a site and subsequent settlement. A noteworthy observation was that the sites switched rank in their settlement rates from 1983 to 1984. This change in settlement rankings matched a switch in rankings for cyprid concentrations. Settlement itself appears to be an important cause of the spatial pattern of cyprid concentrations. Comparing the rates of settlement to estimates of the number of cyprids available at a site suggests that settlement causes a large drain on the cyprid population as a water mass passes over successive sites. No consistent spatial patterns were found in the distribution of other major plankton groups (calanoid copepods) that are similar in size to Balanus cyprids but do not settle. The large differences in settlement rates among these sites were previously shown to be a leading cause of large differences in the structure of benthic barnacle populations. The close correspondence shown here between these large differences in settlement and differences in larval concentrations suggests that nearshore oceanic processes affecting larval arrival contribute to the control of benthic community structure.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00384297
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  • 3
    Electronic Resource
    Electronic Resource
    The identification and characterization of four laccases from the plant pathogenic fungusRhizoctonia solani (1996)
    Springer
    Current genetics 29 (1996), S. 395-403 
    Details
    ISSN: 1432-0983
    Keywords: Laccas ; Phenol-oxidas ; Rhizoctonia solani ; Fungi
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Four distinct laccase genes,lcc1, lcc2, lcc3 andlcc4, have been identified in the fungusRhizoctonia solani. Both cDNA and genomic copies of these genes were isolated and characterized. Hybridization analyses indicate that each of the four laccase genes is present in a single copy in the genome. TheR. solani laccases can be divided into two groups based on their protein size, intron/exon organization, and transcriptional regulation. Three of these enzymes have been expressed in the fungusAspergillus oryzae. Two of the recombinant laccases, r-lccl and r-lcc4, as well as the native lcc4 enzyme were purified and characterized. The purified proteins are homodimeric, comprised of two subunits of approximately 66 kDa for lcc4 and 50–100 kDa for the recombinant lccl protein. These laccases have spectral properties that are consistent with other blue copper proteins. With syringaldazine as a substrate, lcc4 has optimal activity at pH 7, whereas lcc1 has optimal activity at pH 6.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02208621
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  • 4
    Electronic Resource
    Electronic Resource
    The identification and characterization of four laccases from the plant pathogenic fungus Rhizoctonia solani (1996)
    Springer
    Current genetics 29 (1996), S. 395-403 
    Details
    ISSN: 1432-0983
    Keywords: Key words Laccas ; Phenol-oxidas ; Rhizoctonia solani ; Fungi
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract  Four distinct laccase genes, lcc1, lcc2, lcc3 and lcc4, have been identified in the fungus Rhizoctonia solani. Both cDNA and genomic copies of these genes were isolated and characterized. Hybridization analyses indicate that each of the four laccase genes is present in a single copy in the genome. The R. solani laccases can be divided into two groups based on their protein size, intron/exon organization, and transcriptional regulation. Three of these enzymes have been expressed in the fungus Aspergillus oryzae. Two of the recombinant laccases, r-lcc1 and r-lcc4, as well as the native lcc4 enzyme were purified and characterized. The purified proteins are homodimeric, comprised of two subunits of approximately 66 kDa for lcc4 and 50–100 kDa for the recombinant lcc1 protein. These laccases have spectral properties that are consistent with other blue copper proteins. With syringaldazine as a substrate, lcc4 has optimal activity at pH 7, whereas lcc1 has optimal activity at pH 6.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002940050061
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  • 5
    Electronic Resource
    Electronic Resource
    Ethylene receptor expression is regulated during fruit ripening, flower senescence and abscission (1996)
    Springer
    Plant molecular biology 31 (1996), S. 1227-1231 
    Details
    ISSN: 1573-5028
    Keywords: abscission ; ethylene ; receptor ; ripening ; senescence ; tomato
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Using theArabidopsis ethylene receptorETR1 as a probe, we have isolated a tomato homologue (tETR) from a ripening cDNA library. The predicted amino acid sequence is 70% identical toETR1 and homologous to a variety of bacterial two component response regulators over the histidine kinase domain. Sequencing of four separate cDNAs indicates that tETR lacks the carboxyl terminal response domain and is identical to that encoded by the tomatoNever ripe gene. Ribonuclease protection showed tETR mRNA was undetectable in unripe fruit or pre-senescent flowers, increased in abundance during the early stages of ripening, flower senescence, and in abscission zones, and was greatly reduced in fruit of ripening mutants deficient in ethylene synthesis or response. These results suggest that changes in ethylene sensitivity are mediated by modulation of receptor levels during development.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00040839
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  • 6
    Electronic Resource
    Electronic Resource
    Vascularization of the crayfish abdominal nerve cord (1981)
    Springer
    Journal of comparative physiology 143 (1981), S. 93-101 
    Details
    ISSN: 1432-1351
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The anatomy of the vascular supply to the abdominal nerve cord of the crayfishProcambarus clarkii was investigated by filling the arterial supply with ink injected into the heart. The abdominal nerve cord was found to receive all of its blood supply from the ventral artery, which parallels the ventral midline of the nerve cord. Extensive vascularization of the abdominal nerve cord was revealed, with more major arterial inputs entering the ganglia than the connectives (Figs. 2, 3, 6). Both the neuronal somata and the neuropil are heavily vascularized (Figs. 4, 6). The connectives contained little of the fine vascularization found within the ganglia, and the roots were lightly and variably vascularized (Figs. 5, 6). Cannulation of the arterial supply can be used to deliver solutions to synapses within the ganglionic neuropil (Figs. 7, 8). Responses of the lateral giant axon (LG) to root and cord stimuli were used to monitor the effects of ionic substitutions in the bathing medium and arterial perfusate. Polysynaptic pathways containing chemical synapses were unaffected when the bathing medium was high Mg++, low Ca++ saline and the arterial perfusate was normal saline. These same pathways were blocked rapidly by arterial perfusion of high Mg++, low Ca++ saline.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00606072
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  • 7
    Electronic Resource
    Electronic Resource
    The cysteine-rich and C-terminal domains of dystrophin are not required for normal costameric localization in the mouse (1996)
    Springer
    Transgenic research 5 (1996), S. 123-130 
    Details
    ISSN: 1573-9368
    Keywords: dystrophin localization ; homologous recombination ; embryonic stem cells ; in vitro differentiation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Dystrophin has a modular structure and is believed to be critical for muscle cell cytoarchitecture by linking the cytoskeleton to the extracellular matrix. The N-terminus binds to actin and two domains at the C-terminus, the cysteine-rich and C-terminal domains, are associated with the sarcolemma indirectly via the dystroglycan complex. We have generated a mutation in mouse embryonic stem (ES) cells which serves to delete the cysteine-rich and C-terminal domains to address directly their role. We show that these two domains are not necessary for normal costameric organization at the sarcolemma in myotubes derived from the mutant cell line. Furthermore sarcolemmal localization is also apparent in mouse chimaeric musclein vivo.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01969430
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  • 8
    Electronic Resource
    Electronic Resource
    Unequal activities of the two tilapia prolactins in the whole-animal transepithelial potential bioassay using the red eft (1989)
    Springer
    Fish physiology and biochemistry 7 (1989), S. 119-124 
    Details
    ISSN: 1573-5168
    Keywords: prolactin ; bioassay ; hormone variants ; transepithelial potential ; tilapia ; Oreochromis mossambicus ; red eft ; Notophthalmus viridescens
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The cichlid fish tilapia (Oreochromis mossambicus) produces two forms of prolactin (tPRL177 and tPRL188) at equal rates. The primary sequences of this prolactin pair share only 69% identity. In these experiments, the whole-animal transepithelial potential (TEP) in the eft stage of the red-spotted newt (Notophthalmus viridescens) was measured in response to two injections totaling about 2 μg of tPRL177, tPRL188, ovine PRL, or tilapia growth hormone (tGH), or distilled water (5 μL/injection). This investigation was undertaken in order to locate prolactin receptors which discriminate between the two molecular forms of tilapia prolactin. The salamandrid integumental bioassay for prolactin was found to respond to tPRL177 as it does to ovine PRL. The more mainline tPRL188 was without effect at this dose and thus behaved more similarly to growth hormone (tilapia and ungulate) in this bioassay. The suspected magnitude of differences in the molecular surface characteristics between the two prolactins seem to be adequate to allow the binding of tPRL177 and to hinder the binding of tPRL188 to prolactin specific receptors in eft epithelial tissues.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00004697
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  • 9
    Electronic Resource
    Electronic Resource
    Market share and price determination in the contemporary airline industry (1993)
    Springer
    Review of industrial organization 8 (1993), S. 419-433 
    Details
    ISSN: 1573-7160
    Keywords: Airline pricing ; deregulation ; contestability ; hub-and-spoke system
    Source: Springer Online Journal Archives 1860-2000
    Topics: Economics
    Notes: Abstract This paper examines airline pricing and market structure determination for domestic airport-pair routes. The model includes variables to control for the effects of congestion, consumer brand preferences, barriers to entry into airports, and multiple airport availability within a city. The results indicate the noncontestability of airline markets, but certain factors can mitigate a carrier's endpoint dominance. Additionally, the need for policies addressing airport congestion is indicated by several aspects of model results.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01024279
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  • 10
    Electronic Resource
    Electronic Resource
    One third cherokee: Problem solving, teaching, and intuition (1978)
    Springer
    Educational studies in mathematics 9 (1978), S. 391-409 
    Details
    ISSN: 1573-0816
    Source: Springer Online Journal Archives 1860-2000
    Topics: Mathematics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00410585
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