Medizinische Universität Graz Austria/Österreich - Forschungsportal - Medical University of Graz
Gewählte Publikation:
Krebs, A; Zipper, P; Vinogradov, SN.
Lack of size and shape alteration of oxygenated and deoxygenated Lumbricus terrestris hemoglobin?
Biochim Biophys Acta. 1996; 1297(2):115-118
Doi: 10.1016/s0167-4838(96)00141-0
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- 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.
- Find related publications in this database (using NLM MeSH Indexing)
- Animals -
- Annelida - chemistry
- Chemical Phenomena -
- Chemistry -
- Hemoglobins - chemistry
- Hemoglobins - metabolism
- Oxygen - metabolism
- Particle Size -
- Protein Conformation -
- Scattering, Radiation -
- Spectrophotometry -
- X-Rays -
- Find related publications in this database (Keywords)
- hemoglobin
- hexagonal-bilayer molecule
- oxygenation
- shape
- small-angle
- X-ray scattering
- (L-terrestris)