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Lack of normal to fast moving transition in the amino terminal fragment of bovine serum albumin


, : Lack of normal to fast moving transition in the amino terminal fragment of bovine serum albumin. European Journal of Biochemistry 141(3): 473-476

A fragment of bovine serum albumin (BSA) corresponding to positions 1-385 of the protein sequence was prepared by peptic digestion. Acid-induced conformational changes in the fragment as well as in the intact albumin were studied by hydrodynamic and spectral methods. Special emphasis was given to the pH zone, which is known to cause the N-F transition in BSA. In agreement with earlier reports it was shown that BSA undergoes N-F transition in the neighborhood of pH 4.0. Results on the fragment showed that it was unable to exhibit the N-F transition under identical experimental conditions. Since BSA and the peptic fragment differ in that the latter lacks the C-terminal portion (i.e., residues 386-582) of its parent molecule, it is concluded that the separation of the C-terminal region (from the rest of the molecule) and/or its unfolding is probably responsible for the N-F transition in BSA.

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