Modulation of nitric oxide affinity by amino acid residues in the pocket of the β-chains

C. Fronticelli; N. Shoaee

Modulation of nitric oxide affinity by amino acid residues in the pocket of the β-chains

Research output: Contribution to journal › Conference article › peer-review

Abstract

Vasoactivity represents a major concern for the in vivo use of cell free hemoglobin believed to result from the interaction of hemoglobin with the endothelium-derived relaxing factor (EDRF). Strong evidence shows that EDRF is in fact nitric oxide (NO). The high affinity of NO for hemoglobin is due to its extremely low dissociation reaction. An increase in NO dissociation will result in a decreased affinity for NO. These indicate that the affinity for NO can be affected by amino acid substitutions in the heme pocket.

Original language	English (US)
Pages (from-to)	A100
Journal	Artificial Cells, Blood Substitutes, and Immobilization Biotechnology
Volume	22
Issue number	5
State	Published - Nov 1 1994
Externally published	Yes
Event	Proceedings of the 11th Congress of the International Society for Artificial Cells, Blood Substitutes and Immobilization Biotechnology, (ISABI) - Boston, MA, USA Duration: Jul 24 1994 → Jul 27 1994

ASJC Scopus subject areas

Biotechnology
Biomedical Engineering

Cite this

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title = "Modulation of nitric oxide affinity by amino acid residues in the pocket of the β-chains",

abstract = "Vasoactivity represents a major concern for the in vivo use of cell free hemoglobin believed to result from the interaction of hemoglobin with the endothelium-derived relaxing factor (EDRF). Strong evidence shows that EDRF is in fact nitric oxide (NO). The high affinity of NO for hemoglobin is due to its extremely low dissociation reaction. An increase in NO dissociation will result in a decreased affinity for NO. These indicate that the affinity for NO can be affected by amino acid substitutions in the heme pocket.",

author = "C. Fronticelli and N. Shoaee",

year = "1994",

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language = "English (US)",

volume = "22",

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journal = "Artificial Cells, Blood Substitutes, and Immobilization Biotechnology",

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note = "Proceedings of the 11th Congress of the International Society for Artificial Cells, Blood Substitutes and Immobilization Biotechnology, (ISABI) ; Conference date: 24-07-1994 Through 27-07-1994",

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T1 - Modulation of nitric oxide affinity by amino acid residues in the pocket of the β-chains

AU - Fronticelli, C.

AU - Shoaee, N.

PY - 1994/11/1

Y1 - 1994/11/1

N2 - Vasoactivity represents a major concern for the in vivo use of cell free hemoglobin believed to result from the interaction of hemoglobin with the endothelium-derived relaxing factor (EDRF). Strong evidence shows that EDRF is in fact nitric oxide (NO). The high affinity of NO for hemoglobin is due to its extremely low dissociation reaction. An increase in NO dissociation will result in a decreased affinity for NO. These indicate that the affinity for NO can be affected by amino acid substitutions in the heme pocket.

AB - Vasoactivity represents a major concern for the in vivo use of cell free hemoglobin believed to result from the interaction of hemoglobin with the endothelium-derived relaxing factor (EDRF). Strong evidence shows that EDRF is in fact nitric oxide (NO). The high affinity of NO for hemoglobin is due to its extremely low dissociation reaction. An increase in NO dissociation will result in a decreased affinity for NO. These indicate that the affinity for NO can be affected by amino acid substitutions in the heme pocket.

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M3 - Conference article

AN - SCOPUS:17444449636

SN - 1073-1199

VL - 22

SP - A100

JO - Artificial Cells, Blood Substitutes, and Immobilization Biotechnology

JF - Artificial Cells, Blood Substitutes, and Immobilization Biotechnology

IS - 5

T2 - Proceedings of the 11th Congress of the International Society for Artificial Cells, Blood Substitutes and Immobilization Biotechnology, (ISABI)

Y2 - 24 July 1994 through 27 July 1994

ER -

Modulation of nitric oxide affinity by amino acid residues in the pocket of the β-chains

Abstract

ASJC Scopus subject areas

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