Ligand binding kinetics of hemoglobin from the earthworm

K. J. Boelts, Lawrence J Parkhurst

Research output: Contribution to journalArticle

16 Citations (Scopus)

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 languageEnglish (US)
Pages (from-to)637-643
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume43
Issue number3
DOIs
StatePublished - May 7 1971

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Oligochaeta
Carbon Monoxide
Hemoglobins
Ligands
Kinetics
Polymers
Molecular Weight
Molecular weight

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Ligand binding kinetics of hemoglobin from the earthworm. / Boelts, K. J.; Parkhurst, Lawrence J.

In: Biochemical and Biophysical Research Communications, Vol. 43, No. 3, 07.05.1971, p. 637-643.

Research output: Contribution to journalArticle

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