Human serum albumin-bound synthetic hemes as an oxygen carrier: Determination of equilibrium constants for heme binding to host albumin

T. Komatsu, K. Hamamatsu, S. Takeoka, H. Nishide, E. Tsuchida

Research output: Contribution to journalArticlepeer-review

12 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)519-527
Number of pages9
JournalArtificial Cells, Blood Substitutes, and Immobilization Biotechnology
Volume26
Issue number5-6
DOIs
Publication statusPublished - 1998 Jan 1

ASJC Scopus subject areas

  • Biotechnology
  • Biomedical Engineering

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