Lack of size and shape alteration of oxygenated and deoxygenated Lumbricus terrestris hemoglobin?

Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology

Volumn 1297, Issue 2, 1996, Pages 115-118

  Krebs, Angelika ^a   Zipper, Peter ^a   Vinogradov, Serge N ^b  

^a UNIVERSITY OF GRAZ   (Austria)

^b WAYNE STATE UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

Hemoglobin; Hexagonal bilayer molecule; L. terrestris; Oxygenation; Shape; Small angle; X ray scattering

Indexed keywords

HEMOGLOBIN;

ANIMAL TISSUE; ANNELID WORM; ARTICLE; CONTROLLED STUDY; IN VITRO STUDY; NONHUMAN; OXYGENATION; PRIORITY JOURNAL; PROTEIN STRUCTURE; RADIATION SCATTERING;

ANIMALS; ANNELIDA; CHEMISTRY; HEMOGLOBINS; OXYGEN; PARTICLE SIZE; PROTEIN CONFORMATION; SCATTERING, RADIATION; SPECTROPHOTOMETRY; X-RAYS;

ANIMALIA; ANNELIDA; LUMBRICUS TERRESTRIS;

EID: 0030591777     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(96)00141-0     Document Type: Article

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