Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0393754 (HSA)
 2,996 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Human alpha-fetoprotein (AFP) and serum albumin (HSA) were studied by hydrophobic interaction chromatography. A close resemblance was observed both in the native state and after various perturbations (pH, salt and alcohol) indicating a significant similarity in their molecular structures. Both proteins displayed similar hydrophobic properties which apparently were different from those of other globular proteins. In agreement with the domain structure proposed by Brown (1976), our results indicated that surface nonpolar side chains of both the native HSA and AFP produced large hydrophobic areas located solely in crevices.
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PMID:Similarity of hydrophobic properties of alpha-fetoprotein and albumin. 617 69

The binding of hemin to human alpha-fetoprotein has been estimated by means of fluorescence and spectrophotometric titration. Spectrophotometric titration discloses one strong binding site for hemin with an association constant of 1.5 X 10(7) M-1. The binding causes a shift of the absorption maximum to a higher wavelength and a rise in the molar absorption coefficient. Fluorescence reveals that the binding of hemin to human AFP quenches the protein fluorescence, which changes in character from a tryptophan type to a tyrosine type. As postulated by our results, the binding of hemin to human AFP is similar to the binding of hemin to HSA.
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PMID:A spectroscopic study of the hemin-human-alpha-fetoprotein system. 620 48