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Molecular cloning, expression, and functional characterization of a 2Cys-peroxiredoxin in Chinese cabbage (1999)

Cheong, Na Eun ; Choi, Yeon Ok ; Lee, Kyun Oh ; [et al.]

Springer

Plant molecular biology 40 (1999), S. 825-834

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ISSN: 1573-5028

Keywords: 2Cys-peroxiredoxin ; Chinese cabbage ; expression ; functional characterization ; gene cloning

Source: Springer Online Journal Archives 1860-2000

Topics: Biology

Notes: Abstract A cDNA (C2C-Prx) corresponding to a 2Cys-peroxiredoxin (2Cys-Prx) was isolated from a leaf cDNA library of Chinese cabbage. The predicted amino acid sequence of C2C-Prx has 2 conserved cysteines and several peptide domains present in most of the 2Cys-Prx subfamily members. It shows the highest sequence homology to the 2Cys-Prx enzymes of spinach (88%) and Arabidopsis (86%). Southern analysis using the cDNA insert of C2C-Prx revealed that it consists of a small multigene family in Chinese cabbage genome. RNA blot analysis showed that the gene was predominantly expressed in the leaf tissue of Chinese cabbage seedlings, but the mRNA was generally expressed in most tissues of mature plant, except roots. The expression of C2C-Prx was slightly induced by treatment with H2O2 (100μM) or Fe3+/O2/DTT oxidation system, but not by ABA (50 μM) or GA3 (10 μM). The C2C-Prx is encoded as a preprotein of 273 amino acids containing a putative chloroplast-targeting signal of 65 amino acids at its N-terminus. The N-terminally truncated recombinant protein (ΔC2C-Prx) migrates as a dimer in a non-reducing SDS-polyacrylamide gel and as a monomer in a reducing condition. The ΔC2C-Prx shows no immuno cross-reactivity to antiserum of the yeast thiol-specific antioxidant protein, and vice versa. The ΔC2C-Prx prevents the inactivation of glutamine synthetase and the DNA cleavage in the metal-catalyzed oxidation system. In the yeast thioredoxin system containing thioredoxin reductase, thioredoxin, and NADPH, the ΔC2C-Prx exhibits peroxidase activity on H2O2.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1023/A:1006271823973

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Effectiveness factor calculations for immobilized enzyme catalysts (1973)

Fink, David J. ; Na, Tsungyen ; Schultz, Jerome S.

New York, NY [u.a.] : Wiley-Blackwell

Biotechnology and Bioengineering 15 (1973), S. 879-888

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ISSN: 0006-3592

Keywords: Chemistry ; Biochemistry and Biotechnology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology

Notes: The steady state, nonlinear diffusion equations which describe reactions in constrained enzyme solutions are of great interest in many biological and engineering applications. As in other types of nonlinear differential equations, exact analytical solutions do not exist except in some simplified cases. In this paper, a general procedure is presented for solving numerically for the substrate concentration profile and effectiveness factor utilizing the transformation method suggested by Na and Na. Design correlations for enzyme solutions constrained within spherical membranes are included. The use of a unique definition of the Thiele Modulus in these charts permits the clear illustration of the effects of substrate concentration and external mass transfer resistances on the overall effectiveness factor for the catalyst particle.

Additional Material: 3 Ill.