muramidase and isoprene

Allergy to natural rubber latex (NRL) results from exposure to proteins derived from Hevea brasiliensis. Type I latex hypersensitivity is observed in certain occupational and other high-risk groups with frequent exposure to NRL products. This includes health care workers (HCWs), workers in the latex industry, children with spina bifida, and atopic individuals.. Early reliable diagnosis and avoidance are required for better patient care. Standardized reagents are not presently available for in vitro and in vivo testing and treatment of patients with latex allergy. However, a number of allergens have been isolated and characterized from Hevea latex and NRL products. Currently, a total of 11 major and minor allergens are designated by the International Allergen Nomenclature Committee. This article reviews the structural and functional characteristics of these latex allergenic proteins.. NRL-allergenic proteins include those involved in the biosynthesis of polyisoprene and coagulation of latex rubber elongation factor, small rubber particle protein, prohevein, and patatin. Pathogenesis-related proteins include beta-1,3-glucanases, chitinases, and hevamine; and the structural proteins include microhelix protein complex, proline-rich protein, profilins, enolases, and manganese superoxide dismutase. Recombinant allergens demonstrated skin test reactivity in patients with latex allergy. The minimal level of skin test reactivity was about 70 pg/mL for NRL and 1 ng/mL for recombinant allergens. The use of selected recombinant latex allergens (Hev b 5, Hev b 6, and Hev b 7) in skin prick tests identified 93% of allergic individuals, mainly health care workers.. Recombinant latex allergens are clinically reactive and can be produced in a standardized manner, which could potentially provide safe and sensitive reagents for the diagnosis and treatment of type I latex allergy.

Topics: Allergens; beta-Glucosidase; Butadienes; Chitinases; Glucan 1,3-beta-Glucosidase; Hemiterpenes; Hevea; Humans; Latex; Muramidase; Pentanes; Phosphopyruvate Hydratase; Plant Diseases; Plant Proteins; Recombinant Proteins; Rubber; Skin Tests; Superoxide Dismutase

The complexation of lysozyme and sodium (sulfamate carboxylate) isoprene/ethylene oxide (SCIEO) at pH = 7.4 and the release of lysozyme from the complexes in the presence of NaCl were investigated. Through electrostatic and hydrophobic interactions, lysozyme and SCIEO form stable complex nanoparticles. The complexation partially disturbs the structure of lysozyme. Some of the hydrophobic residues of lysozyme are exposed to bind with SCIEO. The complexation leads to loss of most of the lysozyme activity. In the presence of NaCl, lysozyme can be released from the complexes. The released lysozyme molecules recover their native structure and activity completely. In the condition of physiological pH and ionic strength, a sustained and extended release of lysozyme was achieved.

Topics: Animals; Buffers; Butadienes; Cattle; Circular Dichroism; Ethylene Oxide; Female; Hemiterpenes; Hydrogen-Ion Concentration; Light; Muramidase; Osmolar Concentration; Pentanes; Polyethylene Glycols; Scattering, Radiation; Sodium Chloride; Spectrophotometry, Ultraviolet; Sulfonic Acids; Time Factors