Low-Molecular-Weight Oxidants Involved in Disulfide Bond Formation

2012 ◽  
Vol 16 (10) ◽  
pp. 1129-1138 ◽  
Author(s):  
Lloyd W. Ruddock
Keyword(s):  
Molecular Weight ◽  
Disulfide Bond ◽  
Bond Formation ◽  
Low Molecular Weight ◽  
Disulfide Bond Formation

scholarly journals A Relaxed Specificity in Interchain Disulfide Bond Formation Characterizes the Assembly of a Low-Molecular-Weight Glutenin Subunit in the Endoplasmic Reticulum

2008 ◽  
Vol 149 (1) ◽  
pp. 412-423 ◽  
Author(s):  
Alessio Lombardi ◽  
Alessandra Barbante ◽  
Pietro Della Cristina ◽  
Daniele Rosiello ◽  
Chiara Lara Castellazzi ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Endoplasmic Reticulum ◽  
Disulfide Bond ◽  
Bond Formation ◽  
Glutenin Subunit ◽  
Low Molecular Weight ◽  
Disulfide Bond Formation ◽  
Interchain Disulfide Bond

scholarly journals On-column disulfide bond formation of monoclonal antibodies during Protein A chromatography eliminates low molecular weight species and rescues reduced antibodies

mAbs ◽  
2020 ◽  
Vol 12 (1) ◽  
pp. 1829333
Author(s):  
Zhijun Tan ◽  
Vivekh Ehamparanathan ◽  
Tingwei Ren ◽  
Peifeng Tang ◽  
Laurel Hoffman ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Monoclonal Antibodies ◽  
Disulfide Bond ◽  
Bond Formation ◽  
Protein A ◽  
Low Molecular Weight ◽  
Disulfide Bond Formation

scholarly journals Conversion of Bacillus subtilis OhrR from a 1-Cys to a 2-Cys Peroxide Sensor

2008 ◽  
Vol 190 (17) ◽  
pp. 5738-5745 ◽  
Author(s):  
Sumarin Soonsanga ◽  
Jin-Won Lee ◽  
John D. Helmann
Keyword(s):  
Molecular Weight ◽  
Bacillus Subtilis ◽  
Disulfide Bond ◽  
Active Sites ◽  
Xanthomonas Campestris ◽  
Bond Formation ◽  
Cysteine Residue ◽  
Low Molecular Weight ◽  
Disulfide Bond Formation ◽  
Protein Dimer

ABSTRACTOhrR proteins can be divided into two groups based on their inactivation mechanism: 1-Cys (represented byBacillus subtilisOhrR) and 2-Cys (represented byXanthomonas campestrisOhrR). A conserved cysteine residue near the amino terminus is present in both groups of proteins and is initially oxidized to the sulfenic acid. TheB. subtilis1-Cys OhrR protein is subsequently inactivated by formation of a mixed-disulfide bond with low-molecular-weight thiols or by cysteine overoxidation to sulfinic and sulfonic acids. In contrast, theX. campestris2-Cys OhrR is inactivated when the initially oxidized cysteine sulfenate forms an intersubunit disulfide bond with a second Cys residue from the other subunit of the protein dimer. Here, we demonstrate that the 1-CysB. subtilisOhrR can be converted into a 2-Cys OhrR by introducing another cysteine residue in either position 120 or position 124. Like theX. campestrisOhrR protein, these mutants (G120C and Q124C) are inactivated by intermolecular disulfide bond formation. Analysis of oxidized 2-Cys variants both in vivo and in vitro indicates that intersubunit disulfide bond formation can occur simultaneously at both active sites in the protein dimer. Rapid formation of intersubunit disulfide bonds protects OhrR against irreversible overoxidation in the presence of strong oxidants much more efficiently than do the endogenous low-molecular-weight thiols.

scholarly journals Biosynthesis of von Willebrand protein by human endothelial cells: processing steps and their intracellular localization.

1984 ◽  
Vol 99 (6) ◽  
pp. 2123-2130 ◽  
Author(s):  
D D Wagner ◽  
V J Marder
Keyword(s):  
Molecular Weight ◽  
Endothelial Cells ◽  
Golgi Apparatus ◽  
Disulfide Bond ◽  
Bond Formation ◽  
Disulfide Bond Formation ◽  
High Mannose ◽  
Von Willebrand ◽  
Processing Steps ◽  
High Molecular Weight Multimers

Biosynthesis of von Willebrand protein by human umbilical vein endothelial cells involved distinct processing steps marked by the presence of several intermediate molecular species. Examination of endoglycosidase H sensitivity of these intracellular intermediates indicated that the processing steps occurred in at least two separate cellular compartments. In the pre-Golgi apparatus (most probably the endoplasmic reticulum), the high mannose carbohydrates were added onto the precursor monomer chains and the 260,000-mol-wt monomers dimerized by interchain disulfide bond formation. The other processing steps have been localized to the Golgi apparatus and later compartments (e.g., Weibel-Palade bodies). High mannose carbohydrate was converted to the complex type, leading to the appearance of a larger precursor subunit of 275,000 mol wt. The 275,000-mol-wt species was not formed if carbohydrate processing was inhibited by the ionophore monensin. From the large pool of dimers of precursor subunits, the high molecular weight multimers were built. These dimer molecules appeared to have free sulfhydryls which might have been involved in the interdimer disulfide bond formation. Simultaneously with multimerization, the precursor subunits were cleaved to the 220,000-mol-wt form. The cleavage of the pro-sequence was not likely to be an absolute requirement for von Willebrand protein multimerization or secretion, as the 275,000-mol-wt precursor subunit was present in secreted high molecular weight multimers of the protein.

scholarly journals Oxygen-independent disulfide bond formation in VEGF-A and CA9

2021 ◽  
pp. 100505
Author(s):  
Fiana Levitin ◽  
Sandy Che-Eun Serena Lee ◽  
Stephanie Hulme ◽  
Ryan A. Rumantir ◽  
Amy S. Wong ◽  
...  
Keyword(s):  
Disulfide Bond ◽  
Bond Formation ◽  
Disulfide Bond Formation
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