Enhanced Production of Therapeutic Proteins in Plants: Novel Expression Strategies

2019 ◽  
pp. 333-351
Author(s):  
Gowtham Iyappan ◽  
Rebecca Oziohu Omosimua ◽  
Ramalingam Sathishkumar
Keyword(s):  
Therapeutic Proteins ◽  
Enhanced Production

Multiobjective Optimization for Enhanced Production of Therapeutic Proteins in Escherichia coli: Application of Real-Time Dielectric Spectroscopy

2020 ◽  
Vol 59 (50) ◽  
pp. 21841-21853
Author(s):  
Nivedhitha Swaminathan ◽  
Priyanka Priyanka ◽  
Anurag S. Rathore ◽  
Senthilkumar Sivaprakasam ◽  
Senthilmurugan Subbiah
Keyword(s):  
Escherichia Coli ◽  
Multiobjective Optimization ◽  
Real Time ◽  
Dielectric Spectroscopy ◽  
Therapeutic Proteins ◽  
Enhanced Production

Activation of cytochrome c to a peroxidase compound I-type intermediate by H2O2: relevance to redox signalling in apoptosis

2004 ◽  
Vol 71 ◽  
pp. 97-106 ◽  
Author(s):  
Mark Burkitt ◽  
Clare Jones ◽  
Andrew Lawrence ◽  
Peter Wardman
Keyword(s):  
Cytochrome C ◽  
Hydroxyl Radical ◽  
Redox Regulation ◽  
Chemotherapeutic Agents ◽  
Tyrosyl Radical ◽  
Compound I ◽  
Definitive Evidence ◽  
Enhanced Production ◽  
Physico Chemical

The release of cytochrome c from mitochondria during apoptosis results in the enhanced production of superoxide radicals, which are converted to H2O2 by Mn-superoxide dismutase. We have been concerned with the role of cytochrome c/H2O2 in the induction of oxidative stress during apoptosis. Our initial studies showed that cytochrome c is a potent catalyst of 2′,7′-dichlorofluorescin oxidation, thereby explaining the increased rate of production of the fluorophore 2′,7′-dichlorofluorescein in apoptotic cells. Although it has been speculated that the oxidizing species may be a ferryl-haem intermediate, no definitive evidence for the formation of such a species has been reported. Alternatively, it is possible that the hydroxyl radical may be generated, as seen in the reaction of certain iron chelates with H2O2. By examining the effects of radical scavengers on 2′,7′-dichlorofluorescin oxidation by cytochrome c/H2O2, together with complementary EPR studies, we have demonstrated that the hydroxyl radical is not generated. Our findings point, instead, to the formation of a peroxidase compound I species, with one oxidizing equivalent present as an oxo-ferryl haem intermediate and the other as the tyrosyl radical identified by Barr and colleagues [Barr, Gunther, Deterding, Tomer and Mason (1996) J. Biol. Chem. 271, 15498-15503]. Studies with spin traps indicated that the oxo-ferryl haem is the active oxidant. These findings provide a physico-chemical basis for the redox changes that occur during apoptosis. Excessive changes (possibly catalysed by cytochrome c) may have implications for the redox regulation of cell death, including the sensitivity of tumour cells to chemotherapeutic agents.

ENHANCED PRODUCTION OF TRICHODERMA CELLULASES THROUGH RECONSTRUCTION OF CELLULASE GENES

2018 ◽  
Vol 3 (1) ◽  
pp. 49-50
Author(s):  
Kh. A. El- Halafawy ◽  
Ragaa A. Eissa ◽  
H. A. Hamza ◽  
A. I. Fahmi
Keyword(s):  
Enhanced Production

Structural Characterization of Recombinant Therapeutic Proteins by Circular Dichroism

2011 ◽  
Vol 12 (10) ◽  
pp. 1508-1516 ◽  
Author(s):  
Carlo Bertucci ◽  
Marco Pistolozzi ◽  
Angela De Simone
Keyword(s):  
Circular Dichroism ◽  
Structural Characterization ◽  
Therapeutic Proteins ◽  
Circular Dichroïsm

Recent Updates on Molecular Genetic Engineering Approaches and Applications of Human Therapeutic Proteins

2017 ◽  
Vol 18 (3) ◽  
pp. 217-232 ◽  
Author(s):  
Asim Azhar ◽  
Ejaj Ahmad ◽  
Qamar Zia ◽  
Mohammad Owais ◽  
Ghulam Md Ashraf
Keyword(s):  
Genetic Engineering ◽  
Molecular Genetic ◽  
Therapeutic Proteins
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