Self-association of sperm whale metmyoglobin

The solution behavior of sperm whale metmyoglobin in 0.15 I phosphate-chloride buffer, pH 7.2, has been examined by sedimentation equilibrium, frontal gel chromatography, and sedimentation velocity. Results obtained from all three studies are shown to be consistent with a self-association model in w...

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Bibliographic Details
Published in:Archives of Biochemistry and Biophysics
Main Authors: Ward L.D., Winzor D.J.
Format: Article in Journal/Newspaper
Language:English
Published: Elsevier BV 1984
Subjects:
Biophysics
Biochemistry
Molecular Biology
1303 Specialist Studies in Education
1304 Biophysics
1312 Molecular Biology
Sperm whale
Online Access:https://espace.library.uq.edu.au/view/UQ:405233
Description
Summary:The solution behavior of sperm whale metmyoglobin in 0.15 I phosphate-chloride buffer, pH 7.2, has been examined by sedimentation equilibrium, frontal gel chromatography, and sedimentation velocity. Results obtained from all three studies are shown to be consistent with a self-association model in which dimerization of the myoglobin is governed by an association equilibrium constant of 0.068 liter/g (580 m-1) at 20 °C.

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