title: Lack of size and shape alteration of oxygenated and deoxygenated Lumbricus terrestris hemoglobin?
abstract: The giant extracellular hemoglobin of Lumbricus terrestris was investigated in the oxygenated, deoxygenated and reoxygenated state using small angle X-ray scattering. Scattering experiments of the oxygenated state of the protein yielded a radius of gyration of 10.71 +/- 0.02 nm, a maximum diameter of 29.37 +/- 0.21 nm and a volume of 6200 +/- 200 nm3. The values for the deoxygenated state of the hemoglobin are smaller than the values for the oxygenated state, but the differences hardly exceed the limits of error.
authors.affiliation: Institute of Physical Chemistry, University of Graz, Austria.
authors.forename: A
authors.initials: A
authors.lastname: Krebs
authors.forename: P
authors.initials: P
authors.lastname: Zipper
authors.forename: S N
authors.initials: SN
authors.lastname: Vinogradov
mesh_terms: D000818:Animals; D000845:Annelida / Q000737:chemistry*; D055598:Chemical Phenomena; D002621:Chemistry; D006454:Hemoglobins / Q000737:chemistry / Q000378:metabolism*; D010100:Oxygen / Q000378:metabolism*; D010316:Particle Size; D011487:Protein Conformation; D012542:Scattering, Radiation; D013053:Spectrophotometry; D014965:X-Rays
chemical_list: D006454:Hemoglobins; D010100:Oxygen