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 which dimerization of the myoglobin is governed by an association equilibrium constant of 0.068 liter/g (580 M-1) at 20 degrees C.
D000818:Animals; D055598:Chemical Phenomena; D002621:Chemistry; D002850:Chromatography, Gel / Q000379:methods; D006420:Hemeproteins; D046911:Macromolecular Substances; D008786:Metmyoglobin; D012996:Solutions; D014461:Ultracentrifugation; D014907:Whales
D006420:Hemeproteins; D046911:Macromolecular Substances; D012996:Solutions; D008786:Metmyoglobin