TY - JOUR
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, S.
AU - Nishide, H.
AU - Tsuchida, E.
N1 - Funding Information:
This work was partially supported by the Core Research for Evolutional Science and Technology, JST and the Health Science Research Grants (Amficial Blood Project), the Ministry of Health and Welfare, Japan.
Copyright:
Copyright 2018 Elsevier B.V., All rights reserved.
PY - 1998
Y1 - 1998
N2 - 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.
AB - 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.
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U2 - 10.3109/10731199809117472
DO - 10.3109/10731199809117472
M3 - Article
C2 - 9844718
AN - SCOPUS:0032212712
SN - 1073-1199
VL - 26
SP - 519
EP - 527
JO - Artificial Cells, Blood Substitutes, and Immobilization Biotechnology
JF - Artificial Cells, Blood Substitutes, and Immobilization Biotechnology
IS - 5-6
ER -