PMID: 1795700Jul 1, 1991

Study of the structural properties of recombinant leukocyte interferon A by means of fluorescence polarization, circular dichroism, and differential microcalorimetry

Molekuliarnaia biologiia
I V DudichV P Zav'ialov


Human leukocyte interferon-A1 (IFN-alpha A) structure in solution was investigated by fluorescence polarization, circular dichroism and scanning microcalorimetry techniques. Using gel-filtration it was established that at neutral pH values and at concentration not exceeding 0.3 mg/ml IFN-alpha A has a dimeric configuration in solution. At pH below 5, IFN-alpha A exists as a monomer. Using circular dichroism technique the IFN-alpha A molecule was shown to preserve a native structure upon decreasing pH to 3.5. The rotational correlation time of IFN-alpha A molecule in dimeric and monomeric form was measured using fluorescence of DNS, conjugated with the protein, and fluorescence of tryptophan residues. Our data indicate that the shape of IFN-alpha A molecule may be approximated by the rigid ellipsoid of revolution with the axis ratio = 4:1. The intramolecular melting of IFN-alpha A was studied by scanning microcalorimetry and circular dichroism in the acidic pH range. Thermodynamic analysis reveals two independent cooperative transitions. These transitions can be explained by assuming that the IFN-alpha A molecule consists of two structural domains.

Related Concepts

Calorimetry, Differential Scanning
Molecular Sieve Chromatography
Circular Dichroism, Vibrational
Fluorescence Polarization
Hydrogen-Ion Concentration
Protein Conformation
Proteins, Recombinant DNA
Interferon alpha-1

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