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1

Effect of plant growth regulators and different nitrogen sources on NADP-isocitrate dehydrogenase activity of radish cotyledons

100%
Sood C. R., Chanda S. V., Singh Y. D.
Acta Physiologiae Plantarum
|
1998
|
tom 20
|
nr 4
NADP-isocitrate dehydrogenase (NADP-ICDH) activity of radish (Raphanus sativus L.) seedlings pretreated with various plant growth regulators: KiN, GA, and ABA and different nitrogen sources viz. KNO₃, NH₄Cl and NH₄NO₃ in light and dark was investigated. ICDH activity was significantly higher in light than in dark; addition of different nitrogen sources reduced it to a greater extent in NO₃ supplementation. Among hormonal treatment only KiN showed slight promotion with KNO₃ and NH₄NO₃. On the other hand in light KNO₃ and/or NH₄NO₃ promoted ICDH activity and among hormones, KiN significantly promoted the activity in KNO₃ and NH₄NO₃ supplemented seedlings while ABA was effective in NH₄CL. It is suggested that in non-photosynthetic tissues, NADP-ICDH provides both reductant and carbon skeleton for glutamate synthesis.
2

Identification of specific interaction of juvenile hormone binding protein with isocitrate dehydrogenase

84%
Zalewska M., Ozyhar A., Kochman M.
Acta Biochimica Polonica
|
2011
|
tom 58
|
nr 1
Juvenile hormone (JH) is essential for multiple physiological processes: it controls larval development, metamorphosis and adult reproduction. In insect hemolymph more than 99 % of JH is bound to juvenile hormone binding protein (JHBP), which protects JH from degradation by nonspecific hydrolases and serves as a carrier to supply the hormone to the target tissues. In Galleria mellonella hemolymph, JHBP is found in a complex with lipid-binding high molecular weight proteins (HMWP) and this interaction is enhanced in the presence of JH. In this report, we present studies on the interaction of JHBP with low molecular weight proteins (LMWP) in the hemolymph. Using ligand blotting we found that JHBP interacts with a protein of about 44 kDa. To identify the protein that preferentially binds JHBP, a LMWP fraction was applied to a Sepharose-bound JHBP and, after washing, the column was eluted with free JHBP acting as a specific competitor or with carbonic anhydrase as a negative control. The eluted proteins were separated by SDS/PAGE and analyzed by mass spectrometry. Isocitrate dehydrogenase was identified as a component of the supramolecular complex of JHBP with hemolymph proteins.
3

Some enzyme activities of acetate mutants of Yarrowia lipolytica

84%
Robak M., Wojtatowicz M., Rymowicz W.
Bulletin of the Polish Academy of Sciences. Biological Sciences
|
1994
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tom 42
|
nr 2
4

Biochemical changes associated with Brassica juncea seed development. I. Respiratory enzymes

84%
Saroop S., Chanda S. V., Singh Y. D.
Acta Physiologiae Plantarum
|
1996
|
tom 18
|
nr 4
5

Enzymatyczno-spektrofluorymetryczna metoda oznaczania kwasu izocytrynowego w sokach owocowych

67%
Maslowska J., Owczarek A.
Bromatologia i Chemia Toksykologiczna
|
2002
|
tom 35
|
nr 1
61-66
Zawartość kwasu izocytrynowego w naturalnych sokach owocowych oznaczano skojarzoną metodą enzymatyczno-spektro-fluorymetryczną. Badania wykazały, że zawartość tego kwasu w sokach owocowych jest niska i wynosi ok. 30 mg/dm3.
6

Cytochemical study of dehydrogenase activity in two euglenid species of the genus Parastasia Michajlow,1966

67%
Wita I.
Acta Protozoologica
|
1989
|
tom 28
|
nr 1
7
Content available remote

Pasture-feeding of Charolais steers influences skeletal muscle metabolism and gene expression

67%
Cassar-Malek I., Jurie C., Bernard C., Barnola I., Micol D., Hocquette J.-F.
Journal of Physiology and Pharmacology. Supplement
|
2009
|
tom 60
|
nr 3
83-90
8
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Content available

Alteration of plasma membrane NADPH oxidase and NADP-recycling enzymes in cucumber roots stressed with cadmium

67%
Jakubowska D., Kabala K., Reda M., Janicka-Russak M.
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology
|
2013
|
tom 94
|
nr 2
9

Histochemical studies on Fasciola hepatica in mice. II. Oxidoreductase activity in experimentally induced fasciolosis

67%
Kolodziejczyk L.
Acta Parasitologica
|
1996
|
tom 41
|
nr 4
CFW strain white mice were infected with various doses (10, 30, 50 and 100) of Fasciola hepatica metacercariae administered per os. Using histochemical methods, the activity of selected oxidoreductases (α-glycerophosphate dehydrogenase, isocitrate dehydrogenase, succinate dehydrogenase, and cytochrome oxidase) was evaluated in the liver of the mice suffering from acute and chronic fasciolosis. Intensified anaerobic and aerobic respiration was recorded. The host’s compensatory mechanism observed in the form of intensified metabolism, was found to be related to the infection intensity.
10

Histochemical studies on Fasciola hepatica in mice. I. Oxidoreductase activity in juvenile and adult liver flukes

67%
Kolodziejczyk L.
Acta Parasitologica
|
1996
|
tom 41
|
nr 4
Histochemical assays were made to study the activity of the following respiratory enzymes: α-glycerophosphate dehydrogenase, isocitrate dehydrogenase, succinate dehydrogenase, and cytochrome oxidase in tissues of Fasciola hepatica during the parasite’s development in the liver of the definitive host. The respiratory enzyme activity was assessed in the tegument, parenchyma, oral sucker, and in the caecum of juvenile and adult F. hepatica inhabiting the host’s liver parenchyma (infection week 1 to 4) and bile ducts (infection week 5-7), respectively. Changes in the intensity of the parasite’s reaction to the dehydrogenases studied were found to be habitat-dependent (liver parenchyma vs. bile ducts). No cytochrome oxidase activity was detected in F. hepatica tissues.
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