Studies of the limited degradation of mucus glycoproteins. The effect of dilute hydrogen peroxide.
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Summary
It is suggested that attack on the histidine residue, with partial conversion into aspartic acid, is accompanied by scission of the histidyl peptide bond.
- Type
- article
- Published
- 1983-05-01
- Cited by
- 63
- References
- 2
- Access
- Open access
- OpenAlex
- https://openalex.org/W129751175
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:27917192
Keywords
Chemistry, Histidine, Sialic acid, Biochemistry, Threonine
References
No references recorded for this paper.
Cited by
- Chemical Pathways of Peptide Degradation: IX. Metal-Catalyzed Oxidation of Histidine in Model Peptides
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- Oxidative damage to fibronectin. II. The effect of H2O2 and the hydroxyl radical.
- Some non-mucin components of mucus and their possible biological roles.
- Role of free radicals and catalytic metal ions in human disease: an overview.
- Nonenzymatic oxidative cleavage of peptide bonds in apoprotein B-100.
- Covalent modification reactions are marking steps in protein turnover.
- The antioxidant properties of zinc.
- Interactions of oxygen radicals with airway epithelium.
- Acute effects of inhalable particles on the frog palate mucociliary epithelium.
- Protein-RNA cross-linking in the ribosomes of yeast under oxidative stress.
- Metal ions and oxygen radical reactions in human inflammatory joint disease.
- Metal ion-catalyzed oxidation of proteins: biochemical mechanism and biological consequences.
- Mucolysis by ascorbic acid and hydrogen peroxide on compact mucin secreted in pseudomyxoma peritonei.
- The role of tracheobronchial mucus in drug administration to the airways
- Protein oxidation and aging
- Free radical production by the red tide alga,Chattonella antiqua
- The effect of oxidants on neutrophil-mediated degradation of glomerular basement membrane collagen.
- Effect of Nitric Oxide on Hydrogen Peroxide-Induced Damage in Isolated Rabbit Gastric Glands
- Formation of diastereoisomeric 3a-hydroxypyrroloindoles from a tryptophan residue analog mediated by iron (II)-EDTA and L-ascorbate.
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