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

T. Komatsu, K. Hamamatsu, Shinji Takeoka, Hiroyuki Nishide, E. Tsuchida

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

Human serum albumin (HSA) incorporating synthetic tetraphenylporphinatoiron 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-K(g)) ranged from 1.2 x 106 to 1.3 x 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
Publication statusPublished - 1998 Nov

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Equilibrium constants
Binding sites
Heme
Fatty acids
Serum Albumin
Molecular structure
Albumins
Oxygen
Derivatives
Hemin
Molecular Structure
Bilirubin
Fatty Acids
Binding Sites

ASJC Scopus subject areas

  • Biomedical Engineering
  • Hematology
  • Biotechnology
  • Biomaterials

Cite this

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T1 - Human serum albumin-bound synthetic hemes as an oxygen carrier

T2 - Determination of equilibrium constants for heme binding to host albumin

AU - Komatsu, T.

AU - Hamamatsu, K.

AU - Takeoka, Shinji

AU - Nishide, Hiroyuki

AU - Tsuchida, E.

PY - 1998/11

Y1 - 1998/11

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AB - Human serum albumin (HSA) incorporating synthetic tetraphenylporphinatoiron 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-K(g)) ranged from 1.2 x 106 to 1.3 x 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.

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