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  • 1
    Electronic Resource
    Electronic Resource
    Radioimmunoassay of limonin using a tritiated tracer (1980)
    s.l. : American Chemical Society
    Journal of agricultural and food chemistry 28 (1980), S. 543-545 
    Details
    ISSN: 1520-5118
    Source: ACS Legacy Archives
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/jf60229a027
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  • 2
    Electronic Resource
    Electronic Resource
    Determination of the mycotoxin cyclopiazonic acid by enzyme immunoassay (1991)
    s.l. : American Chemical Society
    Journal of agricultural and food chemistry 39 (1991), S. 1887-1891 
    Details
    ISSN: 1520-5118
    Source: ACS Legacy Archives
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/jf00010a041
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  • 3
    Electronic Resource
    Electronic Resource
    Monoclonal antibodies for the enzyme immunoassay of the mycotoxin cyclopiazonic acid (1993)
    s.l. : American Chemical Society
    Journal of agricultural and food chemistry 41 (1993), S. 1076-1080 
    Details
    ISSN: 1520-5118
    Source: ACS Legacy Archives
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/jf00031a012
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  • 4
    Electronic Resource
    Electronic Resource
    Radioimmunoassay for naringin and related flavanone 7-neohesperidosides using a tritiated tracer (1983)
    s.l. : American Chemical Society
    Journal of agricultural and food chemistry 31 (1983), S. 1249-1255 
    Details
    ISSN: 1520-5118
    Source: ACS Legacy Archives
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/jf00120a026
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  • 5
    Electronic Resource
    Electronic Resource
    THE BIOCHEMISTRY AND PHYSIOLOGY OF GIBBERELLINS, VOLS I AND II (Book). (1984)
    Oxford, UK : Blackwell Publishing
    Plant, cell & environment 7 (1984), S. 0 
    Details
    ISSN: 1365-3040
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/1365-3040.ep11592204
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  • 6
    Electronic Resource
    Electronic Resource
    Identification and purification of the calcium-regulated Ca2+-ATPase from the endoplasmic reticulum of a higher plant mechanoreceptor organ (1998)
    Copenhagen : Munksgaard International Publishers
    Physiologia plantarum 102 (1998), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Erythrosin b, a potent inhibitor of the Ca2+-ATPases and the Ca2+-release channel (BCC1) in mechanosensitive tissue of Bryonia dioica Jacq., effectively suppresses a tendril's reaction to touch, suggesting that Ca2+-transporters are involved in signal transduction in this organ. The Ca2+-ATPase located in the endoplasmic reticulum (ER) represents a multiregulated enzyme that is stimulated by calmodulin (CaM), KCl and lysophospholipids. Limited proteolysis of ER-membranes by trypsin results in an irreversible activation of the Ca2+-ATPase and loss of the CaM sensitivity, presumably through removal of an autoinhibitory domain where CaM binds. Mild trypsination mimics the effects of CaM on Vmax and the affinity for Ca2+ and ATP. Irrespective of a trypsin treatment, the enzyme can be additionally stimulated by KCl and lysolipids, indicating that the sites of interaction for these effectors are not located in the domain removed by the protease. CaM-stimulated ATPase activity was purified from microsomal and ER fractions using a combination of CaM-affinity and anion-exchange chromatography. The isolated polypeptide was enzymatically active, showed a calcium-dependent mobility-shift in SDS-PAGE from 109 kDa in the absence of Ca2+ to 104 kDa in the presence of 10 mM CaCl2 and could be radiolabeled with [35S]-CaM. The characteristics of the purified enzyme remained closely similar to those of the ER-bound Ca2+-transporting activity, including the enzymatic data, CaM stimulation, and the sensitivity towards a range of inhibitors.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1034/j.1399-3054.1998.1020411.x
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  • 7
    Electronic Resource
    Electronic Resource
    ATP-driven Ca2+ transport in sealed plasma membrane vesicles prepared by aqueous two-phase partitioning from leaves of Commelina communis (1989)
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 75 (1989), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Sealed plasma membrane vesicles were obtained in high purity from leaves of Commelina communis L. by aqueous two-phase partitioning. Based on the analysis of a range of markers, the preparations (U3+U3′ phases) were shown to be devoid of tonoplast, Golgi and thylakoid membranes, and showed only trace mitochondrial contamination. One-third of the vesicles were oriented inside out and exhibited ATP-driven 45Ca2+ transport [? 15 pkat (mg protein)−1]. Ca2+ uptake into the vesicles had a pH optimum of 7.2 and apparent Km values for Ca2+ of 4.4 μM and for Mg-ATP of 300 μM. Ca2+ uptake, K+, Mg2+-ATPase (EC 3.6.1.3) activity as well as glucan synthase II (EC 2.4.1.34) activity were all maximal at the same equilibrium density (1.17 g cm−3) on continuous sucrose density gradients. The protonophore carbonylcyanide m-chlorophenylhydrazone (CCCP) did not inhibit the ATP-dependent Ca2+ transport into the vesicles, excluding a Ca2+/H+ exchange driven by a proton gradient. ATP-dependent Ca2+ uptake was inhibited by erythrosin B (I50= 0.1 μM), ruthenium red (I50= 30 μM), La3+ (I50= 10 μM) and vanadate (I50= 500 μM), but not by azide, cyanide and oligomycin. The calmodulin antagonists, trifluoperazine (I50= 70 μM) and W-7 (I50= 100 μM) were also inhibitory, However, this inhibition was not overcome by calmodulin. Trifluoperazine and W-7, on the other hand, stimulated Ca2+ efflux from the vesicles rather than inhibit Ca2+ uptake. Our results demonstrate the presence of a Ca2+-ATPase in the plasma membrane of C. communis. In the intact cell, the enzyme would pump Ca2+ out of the cell. Its high affinity for Ca2+ makes it a likely component involved in adjusting low cytoplasmic Ca2+ levels. No indications for a secondary active Ca2+/H+ transport mechanism in the plasma membrane of C. communis were obtained. Both, the nucleotide specificity and the sensitivity towards vanadate. distinguish the Ca2+-ATPase from the H+-translocating K+. Mg2+-ATPase in C. communis plasma membranes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1399-3054.1989.tb05611.x
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  • 8
    Electronic Resource
    Electronic Resource
    Determination of xanthoxin by immunoassay (1988)
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 74 (1988), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: 2-Cis(-)xanthoxin (XA) was linked to bovine serum albumin through a Schiff's base and the adduct stabilized by sodium borohydride reduction. The conjugate (molar coupling ratio: 3 mol XA per mol protein) was highly immunogenic in rabbits. Antisera contained antibodies binding XA with high affinity (Ka= 1.8 × 108M−1). [3H]-XA (2.2 × 1014 Bq mol−1) was synthesized by oxidation of [3H]-XA alcohol with MnO2 and used to set up a radioimmunoassay [RIA, detection limit, 1 pmol; measuring range, 1 to 200 pmol (0.3 to 60 ng) XA]. The sera were also suitable for enzyme-linked-immunosorbent assay (ELISA) using XA-alkaline phosphatase conjugates. The technique was more sensitive [detection limit, 0.1 pmol; measuring range, 0.1 to 50 pmol (0.05 to 15 ng) XA] than the radioimmunoassay, but less precise.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1399-3054.1988.tb04961.x
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  • 9
    Electronic Resource
    Electronic Resource
    Immunological estimation of growth regulator distribution in phototropically reacting sunflower seedlings (1988)
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 74 (1988), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The distribution of immunoassayable xanthoxin (XA), abscisic acid (ABA) and indole-3-acetic acid (IAA) in all parts of sunflower (Helianthus annuus L.) seedlings was determined. During the course of phototropic curvature, including the lag phase (5 min), the distribution of these growth regulators was analyzed in the illuminated and shaded side of the hypocotyl, as well as in the peripheral and central tissues. All three growth regulators showed no detectable asymmetries between the illuminated and shaded hypocotyl halves during the lag phase and early phototropic curvature. Also, no indication for an exchange of XA, ABA or IAA between the peripheral and central tissues was observed. Partial removal of the peripheral cell layers revealed that changes in the growth properties of this tissue, preferentially at the illuminated side of the hypocotyl, are required for the phototropic reaction. Complete removal of the peripheral cell layers abolishes the phototropic response. In dark-incubated, green sunflower seedlings, the loss of sensitivity to phototropic stimulation is correlated with decreasing levels of IAA immunoreactivity, whereas no changes in the levels of ABA- and XA immunoreactivity were recorded. The findings are discussed with respect to the involvement of ABA, XA and IAA in phototropic reactions of green dicotyledonous shoots.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1399-3054.1988.tb04962.x
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  • 10
    Electronic Resource
    Electronic Resource
    ATPase activity in plasmalemma-rich vesicles isolated by aqueous two-phase partitioning from Vicia faba mesophyll and epidermis: Characterization and influence of abscisic acid and fusicoccin (1988)
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 72 (1988), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Plasmalemma-rich microsomal vesicles were prepared from whole leaf and acid-washed epidermal tissue of Vicia faba L. cv. Osnabrücker Markt by aqueous two-phase partitioning in dextran T-500 and polyethylenglycol 1350 aqueous phases. These vesicles were tightly sealed and predominantly right-side out, and contained a K+ -stimulated, mg2+-dependent and vanadate-sensitive ATPase. The enzyme from both tissues exhibited nearly identical properties: pH optimum 6.4, Km for ATP 0.60 mM(whole leaf) and 0.67 mM (epidermis). Vmax -480 nmol (mg protein)1 min1 (whole leaf) and 510 nmol (mg protein)1 min1 (epidermis), I50 (Na3,VO4) 7.5 μM (whole leaf) and 15 μM (epidermis). The enzyme was not inhibited by NO3(50 mM)or sodium azide (I mM). DCCD (20 μM) reduced enzyme activity to 50% (whole leaf) and 58% (epidermis), gramicidin S (20 μM) to 36% (whole leaf) and 41%(epidermis). Ca2+ inhibited the ATPase [I50, C2+: 0.5 mM(whole leaf) and 0.8 mM(epidermis)]. Ca2+ inhibited the ATPase [I50, C2+ 0.5 mM(whole leaf) und 0.8 (epidermis)]. The vanadate-sensitive ATPase from whole leaf and epidermal tissue was slightly but significantly stimulated by fusicoccin (FC) at a concentration (0.13 μM) promoting stomatal opening. The stimulation was not seen in the solubilized ATPase. Stomata of the cultivar used here were insensitive lo (±)ABA up to 2 μM level which is effective in most other cultivars and species. Likewise, at this concentration no effect of ABA on the activity of the epidermal ATPase was observed. The data are discussed with respect to the interaction of FC and ABA with the ATPase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1399-3054.1988.tb05834.x
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