[Study of the binding of iron ions by melanoprotein granules of the eye pigment epithelium using gamma-resonance spectroscopy].
Interaction between Fe2+ ions and melanoproteid granules (MPG) of bovine eye pigment epithelium was studied by gammaresonance spectroscopy. MPG was found to form complexes with bi- and three-valent ferrum ions. MPG can both directly bind Fe2+ ions and oxidize them Fe3+ inactive in prooxidant state and bind the latter. The activity of ferrum ion binding increases when suspension is illuminated with visible light and pH of the incubation solution increases. The protein part of MPG does not participate in the complex formation with ferrum ions. The complex formation proceeds mainly by carboxyl, amino- and imino-groups of melanin polymer.
D000818:Animals; D002417:Cattle; D003594:Cytoplasmic Granules / Q000378:metabolism*; D005136:Eye Proteins / Q000378:metabolism*; D066298:In Vitro Techniques; D007501:Iron / Q000378:metabolism*; D008543:Melanins / Q000378:metabolism*; D010857:Pigment Epithelium of Eye / Q000378:metabolism*; D011506:Proteins / Q000378:metabolism*; D013051:Spectrometry, Gamma
D005136:Eye Proteins; D008543:Melanins; D011506:Proteins; C019464:melanoproteins; D007501:Iron
Issledovanie sviazyvaniia ionov zheleza melanoproteinovymi granulami pigmentnogo épiteliia glaza metodom gamma-rezonansnoĭ spektroskopii.