Effect of iron binding on the conformation of transferrin. A small angle x-ray scattering study

Journal Article · Fri Nov 01 00:00:00 EST 1985 · Biophys. J.; (United States)

DOI:https://doi.org/10.1016/S0006-3495(85)83838-8· OSTI ID:5966230

Kilar, F; Simon, I

Distance distribution functions, p(r), radii of gyration, Rg, and radii of gyration of cross section, Rq, of apotransferrin, monoferric transferrin, and diferric transferrin have been compared. The alteration of Rg and Rq upon iron binding has been determined by a difference method. An unusual feature of the stepwise structural changes of transferrin upon iron saturation is that binding of the first ferric ion is responsible for more than half of the whole change in Rq, whereas Rg alters significantly only after the binding of the second ferric ion.

• Research Organization: Hungarian Academy of Sciences, Budapest
• OSTI ID: 5966230
• Journal Information: Biophys. J.; (United States), Vol. 5
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
37 INORGANIC
ORGANIC
PHYSICAL AND ANALYTICAL CHEMISTRY
TRANSFERRIN
STRUCTURAL CHEMICAL ANALYSIS
CHEMICAL BONDS
IRON
KINETICS
MOLECULAR STRUCTURE
X-RAY DIFFRACTION
COHERENT SCATTERING
DIFFRACTION
ELEMENTS
GLOBULINS
GLOBULINS-BETA
METALLOPROTEINS
METALS
ORGANIC COMPOUNDS
PROTEINS
SCATTERING
TRANSITION ELEMENTS
550200* - Biochemistry
400101 - Activation
Nuclear Reaction
Radiometric & Radiochemical Procedures