scholarly journals Factors influencing serum levels and peritoneal clearances of low molecular weight proteins in continuous ambulatory peritoneal dialysis

1995 ◽  
Vol 48 (6) ◽  
pp. 1946-1952 ◽  
Author(s):  
André Kabanda ◽  
Eric Goffin ◽  
Alfred Bernard ◽  
Robert Lauwerys ◽  
Charles van Ypersele de Strihou
Keyword(s):  
Molecular Weight ◽  
Peritoneal Dialysis ◽  
Continuous Ambulatory Peritoneal Dialysis ◽  
Serum Levels ◽  
Low Molecular Weight ◽  
Factors Influencing ◽  
Low Molecular Weight Proteins

Inhibition of Copper-Associated Erythrocyte Ghost Membrane Lipid Peroxidation by Hepatic Cytosolic Low Molecular Weight Proteins

1991 ◽  
Vol 19 (3) ◽  
pp. 206-213
Author(s):  
Bruce L. Homer ◽  
Kenneth R. Pierce ◽  
Charles H. Bridges ◽  
James E. Womack ◽  
Blair A. Sowa ◽  
...  
Keyword(s):  
Lipid Peroxidation ◽  
Molecular Weight ◽  
Membrane Lipid ◽  
Erythrocyte Ghost ◽  
Low Molecular Weight ◽  
Membrane Lipid Peroxidation ◽  
Low Molecular Weight Proteins

scholarly journals Ether Oxidation by an Evolved Fungal Heme-Peroxygenase: Insights into Substrate Recognition and Reactivity

2021 ◽  
Vol 7 (8) ◽  
pp. 608
Author(s):  
Raul Mireles ◽  
Joaquin Ramirez-Ramirez ◽  
Miguel Alcalde ◽  
Marcela Ayala
Keyword(s):  
Molecular Weight ◽  
Environmental Conditions ◽  
Substrate Recognition ◽  
Enzyme Inactivation ◽  
Biochemical Reaction ◽  
Low Molecular Weight ◽  
Factors Influencing ◽  
Secondary Reactions ◽  
Oxidation Efficiency ◽  
Favorable Conditions

Ethers can be found in the environment as structural, active or even pollutant molecules, although their degradation is not efficient under environmental conditions. Fungal unspecific heme-peroxygenases (UPO were reported to degrade low-molecular-weight ethers through an H2O2-dependent oxidative cleavage mechanism. Here, we report the oxidation of a series of structurally related aromatic ethers, catalyzed by a laboratory-evolved UPO (PaDa-I) aimed at elucidating the factors influencing this unusual biochemical reaction. Although some of the studied ethers were substrates of the enzyme, they were not efficiently transformed and, as a consequence, secondary reactions (such as the dismutation of H2O2 through catalase-like activity and suicide enzyme inactivation) became significant, affecting the oxidation efficiency. The set of reactions that compete during UPO-catalyzed ether oxidation were identified and quantified, in order to find favorable conditions that promote ether oxidation over the secondary reactions.

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