Ligand binding kinetics of hemoglobin from the earthworm

K. J. Boelts; L. J. Parkhurst

doi:10.1016/0006-291X(71)90662-0

Ligand binding kinetics of hemoglobin from the earthworm

K. J. Boelts, L. J. Parkhurst

Research output: Contribution to journal › Article › peer-review

Abstract

Kinetic measurements of CO and O₂ binding by the high molecular weight (ca. 3,000,000) hemoglobin from Lumbricus terrestris reveal that: (1) the high co-operativity is associated with a much lower value for 1′ ("on" constant for CO) than in mammalian hemoglobins and (2) the value of 1′ for the subunits is at least 20 times that for the intact polymer. Co-operativity in O₂ binding is also manifested kinetically in the O₂ dissociation reaction in the absence and presence of CO as a replacement ligand.

Original language	English (US)
Pages (from-to)	637-643
Number of pages	7
Journal	Biochemical and Biophysical Research Communications
Volume	43
Issue number	3
DOIs	https://doi.org/10.1016/0006-291X(71)90662-0
State	Published - May 7 1971

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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title = "Ligand binding kinetics of hemoglobin from the earthworm",

abstract = "Kinetic measurements of CO and O2 binding by the high molecular weight (ca. 3,000,000) hemoglobin from Lumbricus terrestris reveal that: (1) the high co-operativity is associated with a much lower value for 1′ ({"}on{"} constant for CO) than in mammalian hemoglobins and (2) the value of 1′ for the subunits is at least 20 times that for the intact polymer. Co-operativity in O2 binding is also manifested kinetically in the O2 dissociation reaction in the absence and presence of CO as a replacement ligand.",

author = "Boelts, {K. J.} and Parkhurst, {L. J.}",

note = "Funding Information: 1 This work was supported University of Nebraska",

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doi = "10.1016/0006-291X(71)90662-0",

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T1 - Ligand binding kinetics of hemoglobin from the earthworm

AU - Boelts, K. J.

AU - Parkhurst, L. J.

N1 - Funding Information: 1 This work was supported University of Nebraska

PY - 1971/5/7

Y1 - 1971/5/7

N2 - Kinetic measurements of CO and O2 binding by the high molecular weight (ca. 3,000,000) hemoglobin from Lumbricus terrestris reveal that: (1) the high co-operativity is associated with a much lower value for 1′ ("on" constant for CO) than in mammalian hemoglobins and (2) the value of 1′ for the subunits is at least 20 times that for the intact polymer. Co-operativity in O2 binding is also manifested kinetically in the O2 dissociation reaction in the absence and presence of CO as a replacement ligand.

AB - Kinetic measurements of CO and O2 binding by the high molecular weight (ca. 3,000,000) hemoglobin from Lumbricus terrestris reveal that: (1) the high co-operativity is associated with a much lower value for 1′ ("on" constant for CO) than in mammalian hemoglobins and (2) the value of 1′ for the subunits is at least 20 times that for the intact polymer. Co-operativity in O2 binding is also manifested kinetically in the O2 dissociation reaction in the absence and presence of CO as a replacement ligand.

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Ligand binding kinetics of hemoglobin from the earthworm

Abstract

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