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  • 1
    Electronic Resource
    Electronic Resource
    Structure-function relationship for the highly toxic crotoxin from Crotalus durissus terrificus (1992)
    Springer
    European biophysics journal 21 (1992), S. 199-205 
    Details
    ISSN: 1432-1017
    Keywords: Crotoxin ; Structure-function relationship ; Modelling by homology ; X-ray scattering
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Physics
    Notes: Abstract The three-dimensional structure of the highly toxic crotoxin from Crotalus durissus terrificus was modelled based on sequence analysis and the refined structure of calcium-free phospholipase of Crotalus atrox venom. Small-angle x-ray scattering experiments were performed on aqueous solutions of crotoxin. The radial distribution function derived from these scattering experiments and the one calculated from the model structure are in good agreement. Crotoxin consists of a basic and an acidic subunit. The model strongly suggests that the overall folding motif of phospholipases has been preserved in both subunits. The basic domain has an intact active site. The residues that are expected to contact the lipid tails of the phospholipid are different from other phospholipases, but they are all hydrophobic. The acidic domain consists of three independent chains interconnected by disulfide bonds. Compared to other phospholipases the active site for the greater part has been preserved in this domain, but it is not very well shielded from solvent. Most residues normally in contact with the lipid tails of the phospholipid are missing, which might explain the acidic subunit's lack of phospholipase activity. A homology between the third chain of the acidic domain and neurophysins suggests that the acidic domain may act as a chaperone for the basic domain.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00196764
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  • 2
    Electronic Resource
    Electronic Resource
    Changes in invertase activities precede ovary growth induced by gibberellic acid in (1991)
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 81 (1991), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Developing pods of pea (Pisum sativum L. cv. Alaska no 7) were used to study the enzymes of sucrose metabolism. Acid and neutral invertase (EC 3.2.1.26). sucrose synthase (SS, EC 2.4.1.13) and sucrose phosphate synthase (SPS, EC 2.4.1.14) have been localized in the soluble fraction. Acid invertase activity was also present in the insoluble fraction and in pea ovary apoplast. In pea pods, sucrose breakdown was dominated by the invertase pathway. SS specific activity only increased at late stages of parthenocarpic pod development, while SPS did so in pods obtained by pollination. Changes in time course of invertase activities have been correlated with the growth rate of fruits induced to develop either by fertilization or by exogenous application of giberellic acid (GA), 2,4-dichloro-phenoxy acetic acid (2,4-D) or 6-benzylaminopurine (6-BAP). The soluble neutral activities might be associated with pod elongation, while the acid ones were rather related to assimilate import by the induced fruits. Application of gibberellic acid to non-pollinated ovaries significantly enhanced the soluble neutral invertase activity before any ovary outgrowth was detected (up to 2 h after treatment). Within the same period of time. GA-treated ovaries showed a decrease in the acid invertase activity of the soluble fraction and an increase of the acid invertase activity in the apopiast. preceding in time the increment of the acid invertase activity associated with the insoluble fraction. Our results suggest that the early GA response may be mediated through a promotion of processes of protein secretion.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1399-3054.1991.tb08739.x
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  • 3
    Electronic Resource
    Electronic Resource
    Hormone directed sucrose transport during fruit set induced by gibberellins in Pisum sativum (1987)
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 69 (1987), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: A new system has been developed to study hormone-directed transport in intact plants during parthenocarpic fruit set induced by gibberellins. Gibberellic acid (GA3) and gibberellin A1 (GA1) applied to unpollinated ovaries of pea (Pisum sativum L. cv. Alaska) promoted sucrose transport from the leaf to the site of hormone application. In vivo experiments showed an early (30 min) accumulation of [14C]-sucrose in ovaries of pea stimulated by gibberellins. This activation of sucrose transport appears to be mediated by gibberellins (GA1, GA3), increasing both loading of phloem with sucrose in the leaf (source) and sucrose unloading in the ovary (sink). The ability of pea tissue segments to take up sucrose in vitro was not affected by the hormonal treatment.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1399-3054.1987.tb04300.x
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  • 4
    Electronic Resource
    Electronic Resource
    Thermodynamic properties of the dissociation of several α-oxooximes (1990)
    Springer
    Microchimica acta 102 (1990), S. 129-135 
    Details
    ISSN: 1436-5073
    Keywords: α-oxooximes ; dissociation constants ; dissociation enthalpies ; dissociation entropies
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The changes in free energy, enthalpy and entropy for the dissociation of several α-oxooximes (phenylglyoxal aldoxime, glyoxylanilide oxime,N-ethyl-glyoxylanilide oxime and 1-phenyl-1,2-propanedione-2-oxime) have been determined in water-ethanol medium (50% v/v) at 0.5M ionic strength (NaNO3) and 25 °C. The changes in dissociation free energy were calculated from the pK a values determined by glass-electrode potentiometry, and refined by using the programs MINIGLASS and SUPERQUAD. The dissociation enthalpies were determined by direct thermometric titration, and refined by using the programs MINITERM and MULTITERM.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01244295
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  • 5
    Electronic Resource
    Electronic Resource
    Immunolocalization of lipoxygenase in pea (Pisum sativum L.) carpels (1996)
    Springer
    Plant cell reports 15 (1996), S. 620-626 
    Details
    ISSN: 1432-203X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Polyclonal antibodies against a part of pea (Pisum sativum L.) LOXG protein have been raised to study the pattern of distribution of related lipoxygenases in pea carpels. The antiserum recognized three lipoxygenase polypeptides in carpels. One of them became undetectable 24 hours after fruit development induction, suggesting that it may correspond to the protein derived from loxg cDNA. Immunolocalization experiments showed that lipoxygenase protein was present only in pod tissues: it was abundant in the mesocarp and, from the day of anthesis, in the endocarp layers. Lipoxygenase distribution is regulated throughout development. The association of lipoxygenase with cells in which processes of expansion and growth will potentially take place support a role in pod growth and development.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00232465
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  • 6
    Electronic Resource
    Electronic Resource
    Distribution of photoassimilates in the pea plant: chronology of events in non-fertilized ovaries and effects of gibberellic acid (1989)
    Springer
    Planta 180 (1989), S. 53-60 
    Details
    ISSN: 1432-2048
    Keywords: Carbon (short-lived isotope,11C) ; Gibberellin and assimilate distribution ; Ovary growth ; Photoassimilate partitioning ; Pisum (photoassimilate partitioning)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The short-lived isotope11C (t1/2=20.4 min) has been used to study assimilate distribution in intact pea plants (Pisum sativum L.). Radiolabel was measured at the leaf fed with11CO2 (feed-leaf), at the ovary of the flower subtended by this leaf, and in shoot apex and roots of individual plants. Considerable11C-radiolabel was detected in the young ovaries during the first days after anthesis. Thereafter, when the ovaries stopped growing the uptake of11C rapidly decreased. At this developmental stage only apex and roots were competing for the photoassimilates. Fertilization, however, restored the strong sink activity of the ovaries. The same effect could be achieved by applying gibberellic acid to non-fertilized ovaries. About 2 h after treatment the residual11C-radiolabel entering the ovary started to increase and, at about the same time, the ovary resumed growth. Feed-leaf photosynthesis, as well as export of11C-radiolabel out of the leaf, was not changed by the treatment. The11C experiments show the dynamic behaviour of the sinks during developmental stages from the day of anthesis until 5 d later and demonstrate that phytohormones may play an important role in regulating carbon distribution.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02411410
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  • 7
    Electronic Resource
    Electronic Resource
    Immunolocalization of lipoxygenase in pea (Pisum sativum L.) carpels (1996)
    Springer
    Plant cell reports 15 (1996), S. 620-626 
    Details
    ISSN: 1432-203X
    Keywords: Abbreviations: DTT, dithiothreitol; EDTA, ethylenediaminetetraacetic acid; IgG, immunoglobulin G; GA3, gibberellic acid; LOX, lipoxygenase; PAGE, polyacrylamide gel; PVDF, polyvinylidene difluoride; SDS, sodium dodecyl sulfate; Tris, 2-amino-2-hydroxymethyl-1,3-propanediol
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Polyclonal antibodies against a part of pea (Pisum sativum L.) LOXG protein have been raised to study the pattern of distribution of related lipoxygenases in pea carpels. The antiserum recognized three lipoxygenase polypeptides in carpels. One of them became undetectable 24 hours after fruit development induction, suggesting that it may correspond to the protein derived from loxg cDNA. Immunolocalization experiments showed that lipoxygenase protein was present only in pod tissues: it was abundant in the mesocarp and, from the day of anthesis, in the endocarp layers. Lipoxygenase distribution is regulated throughout development. The association of lipoxygenase with cells in which processes of expansion and growth will potentially take place support a role in pod growth and development.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002990050086
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  • 8
    Electronic Resource
    Electronic Resource
    Complexation of Ni (II) and Zn(II) ions by 3-(1-naphthyI)-2-mercaptopropenoic acid (1989)
    Springer
    Microchimica acta 98 (1989), S. 91-99 
    Details
    ISSN: 1436-5073
    Keywords: 3-naphthyl-1–2-mercaptopropenoic acid ; complexation constants ; potentiometry ; MINIGLASS program
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The complexation equilibria between Ni(II) and Zn(II) metal ions with 3-(1-naphthyl)-2-mercaptopropenoic acid (H2NMP) were studied by glass electrode potentiometry, at 25 °C and 1.0 mol·dm−3 in NaClO4 as constant ionic medium in 50% (v/v) water-ethanol solutions. Formation constants for the complexes Ni(NMP), Ni(NMP) 2 2− , Zn(NMP) and Zn(NMP) 2 2− , refined by the MINIGLASS program, are reported.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01244521
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  • 9
    Electronic Resource
    Electronic Resource
    Repression of the pea lipoxygenase gene loxg is associated with carpel development (1995)
    Springer
    Plant molecular biology 27 (1995), S. 887-899 
    Details
    ISSN: 1573-5028
    Keywords: carpel development ; fruit-set ; gibberellins ; lipoxygenase ; pea
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A cDNA clone (loxg) corresponding to a gene repressed during carpel development has been isolated from a cDNA library of unpollinated carpels induced to grow by treatment with gibberellic acid (GA3). The sequences of loxg cDNA and the deduced polypeptide have a high similarity with legume type 2 lipoxygenases, especially with Phaseolus lox1 (78.5% similarity at the protein level) and pea and soybean lox3 (83.6% and 85.4%, respectively). loxg expression is constant in unstimulated carpels but it decreases in carpels induced to keep growing by fertilization or hormone treatment. A similar pattern of repression was observed in lipoxygenase activity of pea and tomato carpels. In situ hybridization studies showed that loxg mRNAs are present in the endocarp and the mesocarp of pea pods; no loxg expression was detectable either in the pod exocarp or in the ovules. Loxg is also expressed in other young growing tissues, especially in flower organs. Nevertheless, the natural pattern of flower and fruit development is associated with loxg repression.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00037017
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  • 10
    Electronic Resource
    Electronic Resource
    Molecular characterization of two stamen-specific genes, tap1 and fil1, that are expressed in the wild type, but not in the deficiens mutant of Antirrhinum majus (1991)
    Springer
    Molecular genetics and genomics 229 (1991), S. 129-136 
    Details
    ISSN: 1617-4623
    Keywords: Antirrhinum majus ; Flower development ; MADS box factors ; Signal peptide ; Flower-specific genes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Deficiens, a homeotic gene involved in the genetic control of flower development, codes for a putative transcription factor. Upon mutation of the gene, petals are transformed to sepals and stamens to carpels, indicating that deficiens is essential for the activation of genes required for petal and stamen formation. In a search for putative target genes of deficiens, several stamen- and petal-specific genes were cloned that are expressed in wild type but not in the deficiens globiferamutant. In this report the molecular characterization of two of these genes, tap1 and fil1, is presented. They are transiently expressed during flower development. In situ hybridization data demonstrate that tap1 is expressed in the tapetum of the anthers and fill in the filament of the stamen and at the bases of the petals. Both genes encode small proteins with N-terminal hydrophobic domains suggesting that they are secreted. We discuss possible functions of the gene products and their relationship to the deficiens gene.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00264221
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