2010
DOI: 10.1016/j.ijbiomac.2010.05.013
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Boron stabilizes peroxide mediated changes in the structure of heme proteins

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Cited by 17 publications
(6 citation statements)
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“…Boron has an unusual chemistry which has been suggested to help stabilize the structures of various macromolecular complexes including the membrane and protein complexes [ 44 – 45 ]. As suggested by Hunt, boron may interact with one-to-four OH groups or a nitrogen group on specific biological ligands, such as the flavin/pyridine nucleotides and serine proteases.…”
Section: Discussionmentioning
confidence: 99%
“…Boron has an unusual chemistry which has been suggested to help stabilize the structures of various macromolecular complexes including the membrane and protein complexes [ 44 – 45 ]. As suggested by Hunt, boron may interact with one-to-four OH groups or a nitrogen group on specific biological ligands, such as the flavin/pyridine nucleotides and serine proteases.…”
Section: Discussionmentioning
confidence: 99%
“…Protein protective property of a substance was determined according to Ali et al [37] method. Hemoglobin solution, O. sanctum extract and mixture (hemoglobin, H 2 O 2 and O. sanctum) were prepared followed by spectral analysis to determine the normal hemoglobin peaks.…”
Section: Spectral Analysismentioning
confidence: 99%
“…Proteins that would be indistinguishable by either charge or hydrodynamic radius can be distinguished. (B) Comparison of data with literature monomer hydrodynamic radius. While most proteins match their monomeric size, myoglobin is likely aggregating under the current conditions.…”
Section: Resultsmentioning
confidence: 99%
“…(B) Comparison of data with literature monomer hydrodynamic radius. 49 52 While most proteins match their monomeric size, myoglobin is likely aggregating under the current conditions.…”
Section: Resultsmentioning
confidence: 99%