Structural properties of alpha-fetoprotein from human cord serum: the protein molecule at low pH possesses all the properties of the molten globule.
Structural studies of alpha-fetoprotein (AFP) from human cord serum have shown that a decrease in pH to 3.1 leads to a considerable conformational rearrangement of the protein molecule. The acid form of AFP belongs to the class of denatured conformations and fulfills all the requirements of the molten globule state. The possible functional role of such a transformation is discussed.
Uversky
V N
VN
Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region.
Kirkitadze
M D
MD
Narizhneva
N V
NV
Potekhin
S A
SA
Tomashevski AYu
D000817:Anilino Naphthalenesulfonates / Q000378:metabolism; D005312:Fetal Blood / Q000737:chemistry*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D066298:In Vitro Techniques; D007231:Infant, Newborn; D015394:Molecular Structure; D011487:Protein Conformation; D011489:Protein Denaturation; D017434:Protein Structure, Tertiary; D013816:Thermodynamics; D000509:alpha-Fetoproteins / Q000737:chemistry* / Q000378:metabolism
D000817:Anilino Naphthalenesulfonates; D000509:alpha-Fetoproteins; C027132:1-anilino-8-naphthalenesulfonate