[HTML][HTML] S-Nitrosohemoglobin is unstable in the reductive erythrocyte environment and lacks O2/NO-linked allosteric function
MT Gladwin, X Wang, CD Reiter, BK Yang… - Journal of Biological …, 2002 - ASBMB
Our previous results run counter to the hypothesis that S-nitrosohemoglobin (SNO-Hb)
serves as anin vivo reservoir for NO from which NO release is allosterically linked to oxygen
release. We show here that SNO-Hb undergoes reductive decomposition in erythrocytes,
whereas it is stable in purified solutions and in erythrocyte lysates treated with an oxidant
such as ferricyanide. Using an extensively validated methodology that eliminates
background nitrite and stabilizes erythrocyte S-nitrosothiols, we find the levels of SNO-Hb in …
serves as anin vivo reservoir for NO from which NO release is allosterically linked to oxygen
release. We show here that SNO-Hb undergoes reductive decomposition in erythrocytes,
whereas it is stable in purified solutions and in erythrocyte lysates treated with an oxidant
such as ferricyanide. Using an extensively validated methodology that eliminates
background nitrite and stabilizes erythrocyte S-nitrosothiols, we find the levels of SNO-Hb in …