Structural properties of α‐fetoprotein from human cord serum: the protein molecule at low pH possesses all the properties of the molten globule
Open Access
- 8 May 1995
- journal article
- Published by Wiley in FEBS Letters
- Vol. 364 (2) , 165-167
- https://doi.org/10.1016/0014-5793(95)00379-n
Abstract
Structural studies of α‐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.Keywords
This publication has 25 references indexed in Scilit:
- Molten globule intermediates and protein foldingEuropean Biophysics Journal, 1991
- Chemistry and Biology of α-FetoproteinPublished by Elsevier ,1991
- PREGNANCY AS A NATURAL MODEL OF ALLOGRAFT TOLERANCETransplantation, 1989
- Expression of alpha-fetoprotein receptors by human T-lymphocytes during blastic transformationMolecular Immunology, 1989
- The molten globule state as a clue for understanding the folding and cooperativity of globular‐protein structureProteins-Structure Function and Bioinformatics, 1989
- Protein folding: Hypotheses and experimentsProtein Journal, 1987
- Nonesterified Fatty Acids: Role in the Molecular Events Linking Endocrinology and Oncology via NutritionTumor Biology, 1987
- α-Fetoprotein in Cancer and Fetal DevelopmentAdvances in Cancer Research, 1979
- Estrogen-binding properties of rat, mouse and man fetospecific serum proteins. Demonstration by immuno-autoradiographic methodsBiochemical and Biophysical Research Communications, 1972
- Alpha-Fetoprotein in Ontogenesis and its Association with Malignant TumorsAdvances in Cancer Research, 1971