hydroxylamine/arábkovka thalova

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Purification and properties of porphobilinogen deaminase from Arabidopsis thaliana.

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Porphobilinogen deaminase (EC 4.3.1.8) has been purified to homogeneity (16,000-fold) from the plant Arabidopsis thaliana in yields of 8%. The deaminase is a monomer of M(r) 35,000, as shown by SDS/PAGE, and 31,000, using gel-filtration chromatography. The pure enzyme has a Vmax. of 4.5 mumol/h per

Determination of indole-3-pyruvic acid levels in Arabidopsis thaliana by gas chromatography-selected ion monitoring-mass spectrometry.

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A rapid and simple method is described for the determination of indole-3-pyruvic acid (IPA) levels in Arabidopsis thaliana by gas chromatography-selected ion monitoring-mass spectrometry (GC-SIM-MS). The method includes derivatization of IPA with hydroxylamine in the crude extract, followed by ethyl

Investigations on the reaction pattern of photosystem II in leaves from Arabidopsis thaliana by time-resolved fluorometric analysis.

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The transients of normalized fluorescence yield induced by an actinic laser flash in dark adapted leaves of Arabidopsis thaliana plants were measured with new equipment, that was developed as part of this work and permits the covarage of a wide time domain of 8 decades from 100 ns to 10 s. The raw

TNT phytotransformation pathway characteristics in Arabidopsis: role of aromatic hydroxylamines.

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Basic knowledge of the plant transformation pathways of TNT will aid phytoremediation design and assessment. While TNT transformation by plant metabolism has been demonstrated in previous studies, the presence and role of hydroxylamines in the transformation pathway has not been sufficiently

Isolation and characterization of a D-cysteine desulfhydrase protein from Arabidopsis thaliana.

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In several organisms D-cysteine desulfhydrase (D-CDes) activity (EC 4.1.99.4) was measured; this enzyme decomposes D-cysteine into pyruvate, H2S, and NH3. A gene encoding a putative D-CDes protein was identified in Arabidopsis thaliana (L) Heynh. based on high homology to an Escherichia coli protein

ECA1 complements yeast mutants defective in Ca2+ pumps and encodes an endoplasmic reticulum-type Ca2+-ATPase in Arabidopsis thaliana.

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To understand the structure, role, and regulation of individual Ca2+ pumps in plants, we have used yeast as a heterologous expression system to test the function of a gene from Arabidopsis thaliana (ECA1). ECA1 encoded a 116-kDa polypeptide that has all the conserved domains common to P-type Ca2+

Conversion of a plant oxidosqualene-cycloartenol synthase to an oxidosqualene-lanosterol cyclase by random mutagenesis.

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A random mutagenesis/in vivo selection approach was applied to generate and identify mutations that alter the product specificity of oxidosqualene-cycloartenol synthase (CAS) from Arabidopsis thaliana. This work complements previous studies of triterpene cyclase enzymes and was undertaken to provide

The Tonoplast H+-ATPase of Acer pseudoplatanus Is a Vacuolar-Type ATPase That Operates with a Phosphoenzyme Intermediate.

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The tonoplast H+-ATPase of Acer pseudoplatanus has been purified from isolated vacuoles. After solubilization, the purification procedure included size-exclusion and ion-exchange chromatography. The H+-ATPase consists of at least eight subunits, of 95, 66, 56, 54, 40, 38, 31, and 16 kD, that did not

Identification of an essential tyrosine residue in the catalytic site of a chitinase isolated from Zea mays that is selectively modified during inactivation with 1-ethyl-3-(3-dimethylaminopropyl)-carbodiimide.

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Chitinase isolated from Zea mays seeds is inactivated by 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide (EDC) in the absence of exogenous nucleophiles. Oligomers of N-acetylglucosamine,N,N',N",N"'-tetra-N-acetylchitotetraose (GlcNAc4), and to a lesser extent, N,N',N"-tri-N-acetylchitotriose (GlcNAc3)

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