Noam J Ship

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It is well established that hemoglobin resulting from red cell lysis binds to haptoglobin in plasma to form a complex. The increased molecular size precludes its filtration by the kidneys, redirecting it toward hepatocellular entry. Chemically cross-linked hemoglobins are designed to be resistant to renal excretion, even in the absence of haptoglobin. The(More)
The discovery that hemoglobin (Hb) in erythrocytes contains a fraction of beta-Cys-93 thiols as the nitrosylated derivative (HbSNO) led to the suggestion that this species is involved in transporting and releasing nitric oxide, which is the signal for local vasodilation. The release of NO from HbSNO requires an electron transfer to facilitate release and to(More)
The role of haptoglobin in liver cell entry of acellular native hemoglobin, and cross-linked human hemoglobin, a potentially useful oxygen-carrier alternative in transfusion medicine, was examined in the recirculating, perfused rat liver preparation. Doses of tritiated native human or beta-chain [trimesoyl-(Lys82)beta-(Lys82)beta] cross-linked human(More)
249 words Introduction: 735 words Discussion: 1249 words Table: 4 Figures: 6 References: 40 This article has not been copyedited and formatted. The final version may differ from this version. DMD Fast Forward. Published on February 14, 2008 as DOI: 10.1124/dmd.107.019174 at A PE T Jornals on O cber 9, 2017 dm D ow nladed from
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