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1

Activity and transcript level of aldehyde oxidase during embryo development and seed maturation of Pisum sativum

100%
Zdunek-Zastocka E.
Acta Biologica Cracoviensia. Series Botanica. Supplement
|
2009
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tom 51
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nr 2
2

Plant molybdoenzymes and their response to stress

63%
Zdunek-Zastocka E., Lips H. S.
Acta Physiologiae Plantarum
|
2003
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tom 25
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nr 4
3

Is xanthine dehydrogenase involved in response of pea plants [Pisum sativum L.] to salinity or ammonium treatment

63%
Zdunek-Zastocka E., Lips H. S.
Acta Physiologiae Plantarum
|
2003
|
tom 25
|
nr 4
4
Artykuł dostępny w postaci pełnego tekstu - kliknij by otworzyć plik
Content available

Molecular cloning and expression analysis of ABA 8'-hydroxylase genes during germination of triticale (X Triticosecale Wittm.) seeds

51%
Fidler J., Zdunek-Zastocka E., Bielawski W.
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology
|
2013
|
tom 94
|
nr 3
5
Artykuł dostępny w postaci pełnego tekstu - kliknij by otworzyć plik
Content available

Regulation of abscisic acid metabolism in relation to the dormancy and germination of cereal grains

51%
Fidler J., Zdunek-Zastocka E., Bielawski W.
Acta Societatis Botanicorum Poloniae
|
2015
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tom 84
|
nr 1
Seed dormancy is of particular importance in the cultivation of cereals, as it directly affects the quality of crop yield. If the dormancy period is too short, this may lead to pre-harvest sprouting, whereas a dormancy period that is too long may cause uneven germination; both of these scenarios are associated with economic losses. Most enzymes engaged in the metabolism of abscisic acid (ABA) have been identified, and significant progress has been made in understanding the role of this phytohormone in the induction and maintenance of dormancy, mainly as a result of research conducted in Arabi-dopsis. Much less is known about the metabolism and function of ABA in cereal grains, especially in relation to dormancy and germination. This review focuses on the regulation of ABA metabolism in dormant and non-dormant cereal grains, in both the dry state and upon imbibition. Moreover, this review describes the influence of factors such as after-ripening, light, temperature, nitric oxide, and reactive oxygen species (ROS) on the dormancy and germination of cereal grains. These factors, with the exception of ROS, appear to affect the level of dormancy and germination of grains through regulation of ABA metabolism.
6

Molecular cloning and functional analysis of the second gene encoding glutamate dehydrogenase in triticale

51%
Grabowska A., Zdunek-Zastocka E., Kutryn E., Kwinta J.
Acta Physiologiae Plantarum
|
2017
|
tom 39
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nr 01
7

Purification, biochemical characterisation, and mass spectrometry analysis of phenylalanine aminopeptidase from the shoots of pea plants

51%
Pyrzyna M., Szawlowska U., Bielawski W., Zdunek-Zastocka E.
Acta Physiologiae Plantarum
|
2011
|
tom 33
|
nr 2
Phenylalanine aminopeptidase (Phe-AP) was isolated from the shoots of 3-week-old pea plants and purified to molecular homogeneity using a four-step purification procedure (ammonium sulphate precipitation, chromatography on DEAE-cellulose, phenyl-sepharose HP, and Protein-Pak Q 8HR HPLC columns). The enzyme was purified 513-fold with a recovery of 8%. The molecular weight of the purified enzyme as determined by SDSPAGE and gel filtration was approximately 60 kDa, and the enzyme appeared to be a monomer. Its pH and temperature optimum were pH 7.5 and 37°C, respectively. The enzyme prefers substrates with Phe at the N-terminus, although a high activity for substrates with N-terminal Tyr, Trp, Leu, and Met was also observed. The activity with Leu-β-naphthylamide was at least two times lower than that with Phe-β-naphthylamide (Phe-β-NA). The Km value for activity with Phe-β-NA was the lowest amongst the substrates tested, and it was 7.5 × 10⁻⁵ M. The activity of Phe-AP was not inhibited by EDTA, 1,10-phenanthroline and pepstatin A. The most effective inhibitors were pHMB and E-64, which modify sulphydryl groups; however, a significant inhibition in the presence of DFP and PMSF, both of which are serine protease inhibitors, was also observed. By applying mass spectrometry analysis, the peptides derived from the purified Phe-AP were assigned to amino acid sequences of the leucine aminopeptidases of N-type (LAPs-N).
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