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1Author    JosieL. Shute, PabloS. Jourdan, RichardL. MansellRequires cookie*
 Title    UDP-Glucose: Glucosyltransferase Activity Involved in the Biosynthesis of Flavonol Triglucosides in Pisum sativum L. Seedlings  
 Abstract    From young, light-grown seedlings o f Pisum sativum L. an enzyme activity catalyzing the glu-cosylation o f kaempferol and quercetin in the 3-position to form the 3-0-triglucoside derivative has been demonstrated. The reaction proceeds from the aglycone via the mono-and diglucoside intermediates. The triglucoside can be produced from any o f the less substituted derivatives with uridine diphosphate-Z)-glucose (U D P G) as the glucosyl donor. Young leaf tissues had much high­ er levels o f glucosyltransferase activity than the petioles and internodes. This is the first report o f the synthesis o f flavonol-3-0-triglucosides in vitro. 
  Reference    Z. Naturforsch. 34c, 738 (1979); received June 25 1979 
  Published    1979 
  Keywords    Pisum sativum, Peas, Flavonols, Triglucosides, Glucosyltransferase 
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 TEI-XML for    default:Reihe_C/34/ZNC-1979-34c-0738.pdf 
 Identifier    ZNC-1979-34c-0738 
 Volume    34 
2Author    Ruth Hracky, Jürgen SollRequires cookie*
 Title    Protein Phosphorylation — Dephosphorylation in the Cytosol of Pea Mesophyll Cells  
 Abstract    Soluble protein kinase and protein phosphatase activities were localized in the cytosol of pea mesophyll cells using protoplasts fractionation techniques. The molecular weights of the phos-phorylated cytosolic proteins, as determined by polyacrylamide gel electrophoresis, were 68, 55, 46, 38, 36, 30, 22 and 12 kDa. Histone and, to a much lesser extent, casein but not phosvitin were accepted as exogenous substrates. In every case serine served as acceptor amino acid for the phosphate residue. The protein phosphorylation activity had an alkaline pH optimum, and showed no response to varying Mg2+, Ca2+, Pn cyclo-AMP or calmodulin concentrations. The kinase activity was competitively inhibited by ADP and pyrophosphate with apparent K t values of 0.5 and 0.17 m M , respectively. High ATP concentrations (1 -4 m M) resulted in a strong decrease of radioactivity in the ,2P labeled proteins. It is proposed that the ratio of protein phosphorylation to protein dephosphorylation is regulated by the ATP to ADP ratio in the cytosol. 
  Reference    Z. Naturforsch. 41c, 856 (1986); received July 9/August 5 1986 
  Published    1986 
  Keywords    Protein Kinase, Protein Phosphatase, Cytosol, Protoplasts, Pisum sativum 
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 TEI-XML for    default:Reihe_C/41/ZNC-1986-41c-0856.pdf 
 Identifier    ZNC-1986-41c-0856 
 Volume    41 
3Author    Kohki Akiyamaa, Kazuyoshi Kawazua, Akio KobayashibRequires cookie*
 Title    Partially N-Deacetylated Chitin Oligomers (Pentamer to Heptamer) are Potential Elicitors for (+)-Pisatin Induction in Pea Epicotyls  
 Abstract    Oligomers (dimer to heptamer) of chitosan and their partially/completely N-acetylated derivatives were examined for (+)-pisatin-inducing activities in pea epicotyl elicitor assay at concentrations ranging from 6.25 to 100 j.ig/ml. The structures of the oligomers were analyzed by 'H NM R and M A L D I TOF MS spectrometers. The chitosan oligomers from dimer to tetramer were inactive, while the pentamer exhibited a moderate activity at 100 |ig/ml. The hexamer showed a pronounced activity at 100 |ag/ml, whereas the oligomer had no activity at the higher concentrations. Although the chitosan heptamer induced a moderate amount of (+)-pisatin (ca. 60 j.ig/g fr. wt.) at 50 (.ig/ml, the oligomer did not elicit pisatin formation at 100 |ig/ml. The dimer to tetramer of both partially N-deacetylated chitin (DAC) and chitin were totally inactive. The DAC pentamers (d.a. 31%, 52%), DAC hexamers (d.a. 26%, 41%), and DAC heptamers (d.a. 26%, 36%) exhibited significant elicitor activities at lower concen­ trations (6.25-25 [.ig/ml) than the native chitosan oligomers. The chitin pentamer to heptamer had weak or no activity. Both glucosamine and N-acetylglucosamine were inactive in the assay. These facts suggest that the DAC pentamer to heptamer may act as elicitors for pisatin induction in pea-fungus interactions. 
  Reference    Z. Naturforsch. 50c, 391—397 (1995); received January 4/January 15 1995 
  Published    1995 
  Keywords    Elicitor, Chitosan, Chitin, Phytoalexin, Pisum sativum 
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 TEI-XML for    default:Reihe_C/50/ZNC-1995-50c-0391.pdf 
 Identifier    ZNC-1995-50c-0391 
 Volume    50 
4Author    F. Rank Terjung, K. Arlheinz, M. AierRequires cookie*
 Title    Nonphotochemical Quenching of Chlorophyll Fluorescence in Higher Plant Leaves Studied by Delayed Fluorescence Decay Measurements  
 Abstract    Delayed chlorophyll fluorescence decay measurements on the second time scale were ap­ plied to investigate the state of photosystem II under different photosynthetic conditions. Leaves adapted to high and low light intensities were used to study the effects of nonphoto­ chemical quenching (energy quenching) on the photosynthetic state. 3-(3,4-dichlorophenyl)-1,1-dimethylurea (DCM U)-treated leaves were used to characterize the photosynthetic state in the absence of a transthylakoid ApH, dithiothreitol (D TT)-treated leaves in the absence of the xanthophyll zeaxanthin. The fast decay components were the most affected by energy quenching as indicated by increased decay times. The slowest decay com ponent was hardly affected, neither in amplitude nor in decay time. The measurem ents indicate a relaxation of energy quenching on the second time scale and the absence of damages in the electron transfer chain of PS II. The constant decay times of the DTT-treated leaf, com parable to those of the DCM U-treated leaf, indicate the obligatory role of zeaxanthin for most of the detected energy quenching. 
  Reference    Z. Naturforsch. 53c, 27—32 (1998); received October 9/October 31 1997 
  Published    1998 
  Keywords    Delayed Fluorescence, Energy Quenching, Pisum sativum, Xanthophyll Cycle 
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 TEI-XML for    default:Reihe_C/53/ZNC-1998-53c-0027.pdf 
 Identifier    ZNC-1998-53c-0027 
 Volume    53 
5Author    Christine Schindler, Ruth Hracky, Jürgen SollRequires cookie*
 Title    Protein Transport in Chloroplasts: ATP is Prerequisit  
 Abstract    The energy requirem ent for protein transport into chloroplast was assayed under conditions that perm it to distinguish whether the posttranslational translocation is dependent on A TP or w hether a m em brane potential across the chloroplast envelope can drive this transport event. A m em brane potential is not required for translocation. A TP can support protein transport in the presence of protonophores and ionophores. Non-hydrolyzable A TP analogues and G TP, CTP, U T P cannot serve as ATP substitutes. Translocation could be observed when an A TP generating system was used to supply ATP. In contrast ATP degrading systems completely abolished translocation. The inner envelope mem brane localized ATP-ase is probably not involved in the transport event. The results suggest that ATP is needed at the outer chloroplast envelope. Inhibition of protein transport by A D P , pyrophosphate and NaF is studied and its con­ sequences discussed. 
  Reference    Z. Naturforsch. 42c, 103 (1987); received August 26 1986 
  Published    1987 
  Keywords    Protein T ransport, ATP-Hydrolysis, Chloroplasts, Envelope, Pisum sativum 
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 TEI-XML for    default:Reihe_C/42/ZNC-1987-42c-0103.pdf 
 Identifier    ZNC-1987-42c-0103 
 Volume    42 
6Author    N. Orbert, G. Rotjohann, David Messdaghi, Wolfgang KowallikRequires cookie*
 Title    Oxygen Uptake during Photosynthesis of Isolated Pea Chloroplasts  
 Abstract    Mass spectrometric analysis of the gas exchange of illuminated leaflets of 10-14 d old pea seedlings revealed not only 160 2-liberation from photosynthetic H2160-splitting, but also uptake of ls0 2, applied to the gas phase of the reaction vessel. Isolated intact chloroplasts of such leaflets suspended in a medium containing N aH C 03 and glycerate 3-phosphate, on irradiation with blue (A. 448 nm) or red (X 679 nm) light also produced 160 2 from water oxidation and consumed 180 2 from the gas phase. The two reactions were saturated at the same quantum fluence rates. Uptake of 18oxygen was not affected by inhibitors of mito­ chondrial respiration (alternative pathway included), such as rotenone (5 x l0 -5 m), antimycin A (5 x l0 ~6 m), KCN (10-3 m), SHAM (10-3 m), or propylgallate (10-3 m). It was, however, absent, when photosynthetic 16oxygen evolution was completely inhibited by DCMU (10-? m). DBMIB (10~5 m), assumed to prevent electron flow from plastoquinone pool to the cyto­ chrome ö6//-complex, suppressed photosynthetic oxygen evolution, but did not impair uptake of 180 2. A similar result was obtained at application of 4 x l0 _e; m antimycin A. The data are interpreted to show a drain off to molecular oxygen of light-excited electrons from the photosynthetic electron transport chain at the site of plastoquinone pool during photosynthesis. This corresponds to chlororespiration, originally described for Chlamydomo-nas in darkness by Bennoun (1982). It is discussed, whether 0 2-uptake during photosynthesis is an additional means for providing ATP for photosynthetic C 0 2-reduction by increasing the proton gradient across the thylakoid membrane. 
  Reference    Z. Naturforsch. 54c, 209—219 (1999); received October 5/November 13 1998 
  Published    1999 
  Keywords    Pisum sativum, Chlororespiration, 18Oxygen Consumption, Photophosphorylation, Intact Isolated Chloroplasts 
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 TEI-XML for    default:Reihe_C/54/ZNC-1999-54c-0209.pdf 
 Identifier    ZNC-1999-54c-0209 
 Volume    54 
7Author    Ernst WeberRequires cookie*
 Title    The Influence of the Sample Size upon the Result of an Analysis of Variance in Long-Stemmed and Short-Stemmed Mutants of Pisum sativum  
 Abstract    The length of the epidermal cells at the 10th intemode was studied by means of the analysis of variance in the normal type and 6 of each long-stemmed and short-stemmed 
  Reference    (Z. Naturforsch. 31c, 216 [1976]; eingegangen am 6. November 1975) 
  Published    1976 
  Keywords    Sample Size, Analysis of Variance, Radiation Induced Mutants, Pisum sativum 
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 TEI-XML for    default:Reihe_C/31/ZNC-1976-31c-0216_n.pdf 
 Identifier    ZNC-1976-31c-0216_n 
 Volume    31 
8Author    Heinz-W Alter, Scheid, Adelheid Ehmke, Thomas HartmRequires cookie*
 Title    Plant NAD-Dependent Glutamate Dehydrogenase. Purification, Molecular Properties and Metal Ion Activation of the Enzymes from Lemna minor and Pisum sativum  
 Abstract    Glutamate dehydrogenase (L-glutamate: N A D + oxidoreductase (deaminating) EC 1.4.1.2) has been purified to homogeneity from Lemna minor and seeds o f Pisum sativum. As established by polyacrylamide gel electrophoresis the Pisum-enzyme constitutes a multiple pattern o f seven char­ ge isoenzymes whereas the Lemna enzyme shows one single protein band. Molecular weights of 230 000 were calculated for both enzymes by sedimentation equilibrium measurements (Pisum-enzyme]I and comparative gel filtration (Lemna-enzyme). Sodium dodecyl sulfate gel electropho­ resis and electron microscopic observations revealed that both enzymes are composed of four identical subunits (molecular weight 58 500) arranged in a tetraedric structure. The amino acid compositions of both enzymes are similar to those of various hexameric glutamate dehydrogen­ ases. The N-terminal amino acid of the Pisum-enzyme is alanine. Both enzymes require Ca2+ for maximal catalytic activity. For the Lemna-enzyme the K0.s values for Ca2+ are 22 /j.m (NADH-de-pendent reaction) and 4 piM (N A D +-dependent reaction), respectively. Ca2+ which to some extent can be replaced by Zn2+ does not affect the enzyme aggregation but seems to govern a reversible equilibrium between catalytically active and inactive enzyme forms. 
  Reference    Z. Naturforsch. 35c, 213—221 (1980); received November 21 1979 
  Published    1980 
  Keywords    Lemna minor, Pisum sativum, Glutamate Dehydrogenase, Purification, Molecular Properties, Me­ tal Ion Activation 
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 TEI-XML for    default:Reihe_C/35/ZNC-1980-35c-0213.pdf 
 Identifier    ZNC-1980-35c-0213 
 Volume    35 
9Author    Z. NaturforschRequires cookie*
 Title    Glutamate Dehydrogenase of Pisum sativum: Heat-Dependent Interconversion of the M ultiple Forms  
 Abstract    Purified NAD-dependent glutamate dehydrogenase (EC 1.4.1.2) from pea seeds shows a pattern o f seven catalytically active molecular forms. The individual forms display different heat stabilities. During incubation at 70 to 75 °C in the presence o f protective agents (N A D H , Ca2+, DTE) the more heat labile forms are converted into the m ost stable form. This result presents direct evidence that the m ultiple forms o f pea glutam ate dehydrogenase represent conform a­ tional variants o f a single protein species. 
  Reference    Z. Naturforsch. 39c, 257 (1984); received N ovem ber 22 1983 
  Published    1984 
  Keywords    Pisum sativum, Glutamate Dehydrogenase, M ultiple Forms, H eat-D ependent Interconversion, Conformational Variants 
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 TEI-XML for    default:Reihe_C/39/ZNC-1984-39c-0257.pdf 
 Identifier    ZNC-1984-39c-0257 
 Volume    39