Human serum albumin (HSA) incorporating synthetic tetraphenylporphinato-iron(II) derivatives (FeP1 or FeP2) can bind and release oxygen reversibly under physiological conditions (in aqueous media, pH 7.4, 37°C). The maximal binding ratio of FeP1/HSA was estimated to be eight, and the stepwise equilibrium constants for FeP1 binding to HSA (K1-K8) ranged from 1.2×106 to 1.3×104 M-1. The major binding sites of FeP1 are presumably identical to those of hemin, bilirubin and long-chain fatty acids. The O2-binding ability of the HSA-FeP can be regulated by changing the molecular structure of the incorporated hemes. The half-lifetime of the O2-coordinated FeP2 in HSA was significantly longer than that of HSA-FeP1.
|Number of pages||9|
|Journal||Artificial Cells, Blood Substitutes, and Immobilization Biotechnology|
|Publication status||Published - 1998 Jan 1|
ASJC Scopus subject areas
- Biomedical Engineering