[Intramolecular structure of mammalian serum albumin].
Some intramolecular peculiarities of the structure of the blood albumin serum of some mammals were studied by means of probe luminescence polarization, phase fluorimetry, and solubilization. It has been shown that microviscosity of the "universal" hydrophobic nucleus where N-phenylnaphtylamine is localized is much above that in the surface regions of the protein globule filled with the probe I-anilinonaphtalene-8-sulphonate (ANS). High values of microviscosity of universal nuclei and surface hydrophobic regions were found in the albumins of man and guinea pig. In protein molecules of rabbit and bull lower microviscosity of probe surroundings was recorded both for the nucleus and peripheral surface regions. Rat albumin had higher microviscosity of ANS localization sites, while the density of the hydrophobic nucleus was comparatively low. At the same time an opposite phenomenon was observed in pig albumin preparations.
Ostolovskiĭ
E M
EM
Botsianskiĭ
A D
AD
Zadorozhnyĭ
B A
BA
D000817:Anilino Naphthalenesulfonates; D000818:Animals; D002417:Cattle; D005456:Fluorescent Dyes; D006168:Guinea Pigs; D006801:Humans; D011487:Protein Conformation; D011817:Rabbits; D051381:Rats; D012709:Serum Albumin / Q000737:chemistry*; D013050:Spectrometry, Fluorescence; D013552:Swine
D000817:Anilino Naphthalenesulfonates; D005456:Fluorescent Dyes; D012709:Serum Albumin; C027132:1-anilino-8-naphthalenesulfonate
O vnutrimolekuliarnoĭ strukture syvorotochnogo al'bumina mlekopitaiushchikh.