Ceruloplasmin has two nearly identical sites that bind myeloperoxidase
نویسندگان
چکیده
منابع مشابه
Ceruloplasmin is an endogenous inhibitor of myeloperoxidase.
Myeloperoxidase is a neutrophil enzyme that promotes oxidative stress in numerous inflammatory pathologies. It uses hydrogen peroxide to catalyze the production of strong oxidants including chlorine bleach and free radicals. A physiological defense against the inappropriate action of this enzyme has yet to be identified. We found that myeloperoxidase oxidized 75% of the ascorbate in plasma from...
متن کاملHow shaped light discriminates nearly identical biochromophores.
We present a general mechanism for successful discrimination of spectroscopically indistinguishable biochromophores by shaped light. For this purpose we use nonadiabatic dynamics in excited electronic states in the frame of the field-induced surface hopping method driven by the experimentally shaped laser fields. Our findings show that optimal laser fields drive low-frequency vibrational modes ...
متن کاملDirect Product Testing With Nearly Identical Sets
In this work we analyze a direct product test in which each of two provers receives a subset of size n of a ground set U , |U | = Θ(n), and the two subsets intersect in about (1 − δ)n elements. We show that if each of the provers provides labels to the n elements it received, and the labels of the two provers agree in the intersection between the subsets with non-negligible probability, then th...
متن کاملInteraction of coatomer with aminoglycoside antibiotics: evidence that coatomer has at least two dilysine binding sites.
Coatomer is the soluble precursor of the COPI coat (coat protein I) involved in traffic among membranes of the endoplasmic reticulum and the Golgi apparatus. We report herein that neomycin precipitates coatomer from cell extracts and from purified coatomer preparations. Precipitation first increased and then decreased as the neomycin concentration increased, analogous to the precipitation of a ...
متن کاملSimultaneous Detection of Multiple Proteins that Bind to the Identical Ligand in Supported Lipid Bilayers.
Herein, we developed a new separation-based detection method that is capable of simultaneously identifying multiple competitively binding proteins for the same ligand on supported lipid bilayers (SLBs). This strategy used unlabeled target analyte proteins that bind to fluorescently tagged, lipid-conjugated ligands within the SLB. The protein-ligand binding complexes were then focused under an a...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Biochemical and Biophysical Research Communications
سال: 2014
ISSN: 0006-291X
DOI: 10.1016/j.bbrc.2014.09.134