title: Allergenic proteins are fragmented in low concentrations of sodium hypochlorite.
abstract: BACKGROUND
  To facilitate allergen removal from indoor environments, it would be helpful to have household cleaning products that modified allergenic activity. Because NaOCl dissolves proteins in high concentrations and is both capable of killing bacteria and viruses and inactivating viral antigens at somewhat lower concentrations, we explored its effects on Mus m 1 and other indoor allergens.
  
  
  OBJECTIVE
  To examine the ability of NaOCl to reduce the allergenicity of Mus m 1 and other indoor allergens.
  
  
  METHODS
  Using purified mouse urinary allergen, we examined the effect on protein measured by Coomassie protein assay and on Mus m 1 measured by ELISA. We also examined the effects using SDS/PAGE and Western blots probed with sheep anti-Mus m 1 and with allergic human serum.
  
  
  RESULTS
  When NaOCl and Mus m 1 were combined in a molar ratio of 100 : 1, IgE binding to Mus m 1 on Western blot was significantly reduced. At higher NaOCl concentrations the protein appeared to fragment and eventually became undetectable. Fragmentation appeared to be random in that peptides of a wide range of apparent molecular weight were produced. The reaction was complete within 1-2 min at OCl : pr ratios of greater than 200 : 1 and was optimal at pH 7.4. Immunological activity of other allergens (Fel d 1, Bla g 1, Der p 1) was decreased in vitro and dried allergen extracts were removed from surfaces. Adding an extraneous protein, BSA, to NaOCl:Mus m 1 solutions decreased the effect of NaOCl on the allergen.
  
  
  CONCLUSIONS
  We concluded that NaOCl at concentrations commonly used in household products is capable of dramatically affecting allergenic protein.
authors.affiliation: Johns Hopkins University, 600 North Wolfe Street, Baltimore, MD 21287, USA.
authors.forename: P
authors.initials: P
authors.lastname: Chen
authors.forename: P A
authors.initials: PA
authors.lastname: Eggleston
mesh_terms: D000485:Allergens / Q000378:metabolism*; D000818:Animals; D039741:Antigens, Dermatophagoides; D052179:Antigens, Plant; D002713:Chlorine / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D006023:Glycoproteins / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008297:Male; D051379:Mice; D008810:Mice, Inbred C57BL; D010446:Peptide Fragments / Q000276:immunology / Q000302:isolation & purification / Q000378:metabolism*; D011506:Proteins / Q000378:metabolism; D012967:Sodium Dodecyl Sulfate / Q000378:metabolism; D012973:Sodium Hypochlorite / Q000378:metabolism
chemical_list: D000485:Allergens; D039741:Antigens, Dermatophagoides; D052179:Antigens, Plant; D006023:Glycoproteins; D010446:Peptide Fragments; D011506:Proteins; C105482:allergen Bla g 1; C035737:major urinary proteins; D012967:Sodium Dodecyl Sulfate; D002713:Chlorine; D012973:Sodium Hypochlorite; C059296:Fel d 1 protein, Felis domesticus