[Conformational transitions of human serum albumin depending on pH. Study using tritium markers].
Accessible surfaces of the HSA molecule in N-, F- and B-forms were studied in the present work by tritium labelling method which allowed to obtain detailed information on N-F- and N-B-transitions. In was shown that the F-form in comparison top the N-form is characterized by more high accessibility of Ser, Ala, Ile, Tyr, Phe, His, Arg, Pro, Val and Phe residues and in the B-form Tyr, Ser, Arg, Gly, Ile, Phe and Pro residues turn to be highly accessible. Full accessible surfaces of protein molecule at N-F- and N-B-transitions increase respectively from 39,000 to 70,400 A2 and from 39,000 to 47,000 A2. Basing on the prevailing increase of hydrophobic residues accessibility it is supposed that the molecule expansion testifies the separation of the subunits forming the molecule.
Dzhafarov
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D000596:Amino Acids / Q000737:chemistry; D006801:Humans; D006863:Hydrogen-Ion Concentration; D011487:Protein Conformation; D012709:Serum Albumin / Q000737:chemistry*; D014316:Tritium
D000596:Amino Acids; D012709:Serum Albumin; D014316:Tritium
Zavisiashchie ot pH konformatsionnye perekhody syvorotochnogo al'bumina cheloveka. Issledovanie metodom tritievoĭ metki.