Compatibility in vitro of albumin‐heme (O₂ carrier) with blood cell components

Abstract Recombinant human serum albumin including 2‐[8‐{N‐(2‐methylimidazolyl)}octanoyloxymethyl]‐5,10,15,20‐tetrakis(α,α,α,α‐o‐pivaloylamino)phenylporphinatoiron(II) (albumin‐heme; rHSA‐FeP) is a synthetic hemoprotein that has sufficient capability to reversibly bind and release O₂ under physiological conditions (pH 7.3, 37°C) similar to hemoglobin and myoglobin. In order to use this albumin‐based O₂ carrier as a new class of red blood cell substitutes, its compatibility with blood cell components carefully was investigated in vitro. After the addition of the rHSA‐FeP solution into whole blood at 10, 20, and 44 vol %, the FeP concentration in the plasma phase remained constant for 6 h at 37°C in each group, and no significant time dependence was observed in the numbers of red blood cells, white blood cells, or platelets. The microscopic observations clearly showed that the shapes of the red blood cells had not been deformed during the measurement period. With respect to the blood coagulation parameters (prothrombin time and activated partial thromboplastin time), the coexistence of rHSA‐FeP had only a negligibly small influence. Also the blood compatibility under dynamic flow conditions was evaluated using a microchannel array flow analyzer. All these results suggest that the albumin‐heme has no effect on the morphology of blood cell components in vitro. © 2003 Wiley Periodicals, Inc. J Biomed Mater Res 66A: 292–297, 2003