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  • 1
    Online Resource
    Online Resource
    Hannover : Univ., Inst. für Zierpflanzenbau, Baumschule u. Pflanzenzüchtung, Abt. Spezielle Ertragsphysiologie
    Keywords: Forschungsbericht
    Type of Medium: Online Resource
    Pages: Online-Ressource (30 S., 5,41 MB) , Ill., graph. Darst
    Language: German
    Note: Förderkennzeichen BMBF 50 WB 0010/ 50 BW 0010. - Literaturangaben , Unterschiede zwischen dem gedruckten Dokument und der elektronischen Ressource können nicht ausgeschlossen werden , Auch als gedr. Ausg. vorh , Systemvoraussetzungen: Acrobat reader.
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  • 2
    ISSN: 1432-2048
    Keywords: Auxin-binding protein ; Glycine max L ; Guanosine nucleotides ; Phospholipase A2 ; Signal transduction
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The molecular mechanism of membrane-associated reactions induced by auxin was investigated in membranes isolated from cultured cells of soybean (Glycine max L.). Auxins increased the activity of phospholipase A2 in microsomes isolated from suspensioncultured soybean cells. The reaction was measured as the accumulation of radioactive lysophosphatidylcholine hydrolyzed from radioactive phosphatidylcholine in membranes which had been prelabelled with [14-C]choline in vivo. Stimulation by auxin was detectable after 1 min and was auxin-specific in that weak auxins had little effect. Auxin concentrations as low as 2·10−8 M and up to 2·10+3 M α-naphthaleneacetic acid already stimulated the phospholipase A2 activity. Guanosine and adenosine diphosphate at 100 μM, if applied during homogenization of cells, completely abolished the stimulation of phospholipase A2 by auxin and, when applied after homogenization, had no effect. Guanosine and adenosine 5′-O-thiotriphosphate, uridine 5′-diphosphate, and uridine 5′-triphosphate, all at 100 μM, had no effect in either treatment, suggesting that only nucleotides entrapped in the vesicles could exert an effect. The effect of auxin on phospholipase A2 had an optimum at pH 5.5 and was abolished completely by an antibody against the membrane-associated auxin-binding protein from maize coleoptiles, applied after homogenization. This antibody recognized a 22-kDa polypeptide in highly purified plasma membranes from cultured soybean cells. This suggests a receptor function for this auxin-binding protein and a role for a cytosolic nucleotide-binding protein in the activation of phospholipase A2 by auxin. It is concluded that phospholipase A2 has a function in plant signal transduction.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1432-2048
    Keywords: Key words: Auxin ; Auxin inhibitor ; Cucurbita ; Elongation growth ; Phospholipase A inhibitor ; Signal transduction
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract. Auxin and elicitors reportedly activate phospolipase A. A number of inhibitors known to inhibit animal phospholipase A2 were tested for their ability to inhibit hormone and fusicoccin-induced growth. To this end, growth induced by indolyl-3-acetic acid and 2,4-dichlorophenoxyacetic acid in hypocotyl segments of etiolated zucchini (Cucurbita pepo L.) seedlings was determined in the presence of the inhibitors nordihydroguajaretic acid (NDGA), aristolochic acid, 5,8,11,14-eicosatetraynoic acid (ETYA), PBx (a prostaglandin derivative), and oleylethyl phosphocholine. Each chemical proved inhibitory to auxin-induced growth, oleylethyl phosphocholine being the least effective. The effects of the first three inhibitors were investigated in more detail. Growth induced by 10 μM 2,4-dichlorophenoxyacetic acid or 1 μM indolyl-3-acetic acid was inhibited 50% by about 30–50 μM NDGA, by about 25 μM aristolochic acid, and by about 10–20 μM EYTA. Growth inhibition was reversible and became apparent 0.5–1 h after inhibitor addition. Growth induced by 0.5 or 1 μM fusicoccin was much less inhibited by NDGA and by ETYA, whereas aristolochic acid was only slightly less effective on fusicoccin-induced than on auxin-induced growth. These three inhibitors were also tested for their effects on gibberellin-induced growth in light-grown peas (Pisum sativum L.) and on cytokinin-induced expansion growth in excised cotyledons from radish (Raphanus sativum L.) seedlings. In both tests, aristolochic acid had toxic side-effects although gibberellin-induced growth was still apparent. In the gibberellin test, neither NDGA at up to 100 μM nor ETYA at 80 μM was inhibitory to hormone-induced growth. Moreover, 40 μM ETYA was not inhibitory to kinetin-induced growth. We hypothesize that the selectivity of phospholipase A2 inhibitors for auxin-induced growth implies a different signal transduction pathway for each of the different signal substances tested, and that auxins might use fatty acid(s) and/or lysophospholipid(s) or their derivatives as the preferred second messengers.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1432-203X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract ATP-dependent H+ transport in microsomes from zucchini hypocotyls is stimulated by the ether lipid 1-0-alkyl-2-acetyl-sn-glycero-3-phosphocholine (platelet-activating factor = PAF) known as a hormone-like substance from mammals. The stimulation can only be observed when soluble cytosolic proteins are present. A soluble protein mediating the PAF-dependent H+ transport and a PAF-stimulated protein kinase are coeluted by DEAE-Sephacel chromatography. Stimulation of phosphorylation by PAF of a 55 kDa polypeptide without Ca2+ and, additionally, of a 35 kDa polypeptide in the presence of Ca2+ is observed in zucchini microsomal membranes. This is evidence for a novel phospholipid-stimulated protein kinase in plants. Phosphorylation of regulatory proteins may be involved in the stimulation of in vitro H+ transport by PAF.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Planta 161 (1984), S. 394-397 
    ISSN: 1432-2048
    Keywords: Acid growth theory ; ATPase ; Auxin (action mechanism) ; Cucurbita
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The effect of auxin on membrane-bound ATPase activity was studied in a plasma membrane-enriched fraction from zucchini hypocotyls. The apparent KM of ATPase activity for ATP was decreased in the presence of 10-6 M auxin so that at very low ATP concentrations the stimulation of ATPase activity was most obvious. The weak auxin analogue, 2,3-dichlorophenoxyacetic acid, stimulated much less than the active auxin 2,4-dichlorophenoxyacetic acid.
    Type of Medium: Electronic Resource
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  • 6
    ISSN: 1432-2048
    Keywords: Cucurbita ; ATPase (protonated) ; Plasma membrane (H+-ATPase) ; Vacuole (H+-ATPase)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A new method of preparing sealed vesicles from membrane fractions of pumpkin hypocotyls in ethanolamine-containing buffers was used to investigate the subcellular localization of H+-ATPase measured as nigericin-stimulated ATPase. In a fluorescence-quench assay, the H+ pump was directly demonstrated. The H+ pump was substrate-specific for Mg·ATP and 0.1 mM diethylstilbestrol completely prevented the development of a Δ pH. The presence of unsupecific phosphatase hampered the detection of nigericin-stimulated ATPase. Unspecific phosphatases could be demonstrated by comparing the broad substrate specificity of the hydrolytic activities of the fractions with the clear preference for Mg·ATP as the substrate for the proton pump. Inhibitor studies showed that neither orthovanadate nor molybdate are absolutely specific for ATPase or acid phosphatase, respectively. Diethylstilbestrol seemed to be a specific inhibitor of ATPase activity in fractions containing nigericin-stimulated ATPase, but it stimulated acid phosphatase which tended to obscure its effect on ATPase activity. Nigericin-stimulated ATPase had its optimum at pH 6.0 and the nigericin effect was K+-dependent. The combination of valinomycin and carbonylcyanide m-chlorophenylhydrazone had a similar effect to nigericin, but singly these ionophores were much less stimulatory. After prolonged centrifugation on linear sucrose gradients, nigericin-stimulated ATPase correlated in dense fractions with plasma membrane markers but a part of it remained at the interphase. This lessdense part of the nigericin-stimulated ATPase could be derived from tonoplast vesicles because α-mannosidase, an enzyme of the vacuolar sap, remained in the upper part of the gradient. Nigericinstimulated ATPase did not correlate with the mitochondrial marker, cytochrome c oxidase, whereas azide inhibition of ATPase activity did.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    Planta 203 (1997), S. S107 
    ISSN: 1432-2048
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Springer
    Planta 151 (1981), S. 434-438 
    ISSN: 1432-2048
    Keywords: ATPase ; Auxin ; Cucurbita ; Hypocotyl ; Membrane fractionation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Membrane fractions from Cucurbita maxima hypocotyls were isolated in a medium which inhibits the action of endogenous phospholipases. After removal of soluble phosphatases by Sepharose 2B-CL column chromatography, an auxin-stimulated ATPase activity was found in membrane fractions from linear sucrose gradients. In the presence of 10-4 M phenylacetic acid (PAA), the stimulation by indol-3-acetic acid (IAA) exhibited a bimodal concentration dependence with maximal stimulation of about 50% at 10-6 M IAA. Without PAA, only a high concentration of 10-4 M IAA was stimulatory, whereas 10-6 M IAA had no apparent effect and 10-8 M IAA exhibited weak inhibition. PAA alone had only weak or no effects. The effects of IAA must be considered as hormone-specific. The ATPase activity in the presence of 10-4 M PAA was activated only by 2,4-dichlorophenoxyacetic acid (2,4-D), an active auxin analogue, but not by the inactive stereoisomers, 2,3-D and 3,5-D. Comparison with marker enzyme profiles suggested that part of the auxin-stimulated ATPase was localized on plasma membranes as well as other compartments. Thus, the auxin-stimulated ATPase may become a useful tool in the investigation of the mechanism of action of auxin.
    Type of Medium: Electronic Resource
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  • 9
    ISSN: 1432-203X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Addition of the animal ether phospholipid platelet-activating factor, 1-0-alkyl-2-acetyl-sn-glycero-3-phosphocholine, (PAF) stimulates medium acidification in cultured soybean (Glycine max L.) cells. The pH of the medium after 8–10 hours is on the average one pH unit lower than in controls. With fusicoccin an average pH difference of 1.7 units is reached. Phospholipids, glycerol, 1-oleyl-2-acetyl-sn-glycerol, 1-0-hexadecyl-sn-glycerol, and triolein at the same concentrations as PAF had no stimulatory effect on medium acidification. The detergents CHAPS and deoxycholate lead to alkalinization of the medium whereas lysophosphatidylcholine (LPC), a detergent with structural similarity to PAF, shows no effect.
    Type of Medium: Electronic Resource
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  • 10
    ISSN: 1432-2048
    Keywords: Cucurbita (phospholipid) ; Ether phospholipid ; H+ transport ; Platelet activating factor
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A plant lipid was isolated from zucchini (Cucurbita pepo L.) membranes and from soybean (Glycine max [L.] Merr) phospholipids by thinlayer chromatography and further purified by high-performance liquid chromatography. This plant lipid was chromatographically very similar to the platelet-activating factor, an ether phospho-lipid with hormone-like properties found in mammals. Both the plant lipid and the platelet-activating factor stimulated ATP-dependent H+ transport in isolated membrane vesicles from zucchini hypocotyls.
    Type of Medium: Electronic Resource
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