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

研究成果: Article

11 引用 (Scopus)

抄録

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.

元の言語English
ページ(範囲)519-527
ページ数9
ジャーナルArtificial Cells, Blood Substitutes, and Immobilization Biotechnology
26
発行部数5-6
出版物ステータスPublished - 1998 11

Fingerprint

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

これを引用

@article{a4a499c27f5343f4a8f0232da26129f2,
title = "Human serum albumin-bound synthetic hemes as an oxygen carrier: Determination of equilibrium constants for heme binding to host albumin",
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.",
author = "T. Komatsu and K. Hamamatsu and Shinji Takeoka and Hiroyuki Nishide and E. Tsuchida",
year = "1998",
month = "11",
language = "English",
volume = "26",
pages = "519--527",
journal = "Artificial Cells, Nanomedicine and Biotechnology",
issn = "2169-1401",
publisher = "Informa Healthcare",
number = "5-6",

}

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, Shinji

AU - Nishide, Hiroyuki

AU - Tsuchida, E.

PY - 1998/11

Y1 - 1998/11

N2 - 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.

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.

UR - http://www.scopus.com/inward/record.url?scp=0032212712&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0032212712&partnerID=8YFLogxK

M3 - Article

C2 - 9844718

AN - SCOPUS:0032212712

VL - 26

SP - 519

EP - 527

JO - Artificial Cells, Nanomedicine and Biotechnology

JF - Artificial Cells, Nanomedicine and Biotechnology

SN - 2169-1401

IS - 5-6

ER -