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Comparative study of physicochemical properties of two pike parvalbumins by means of their intrinsic tyrosyl and phenylalanyl fluorescence


, : Comparative study of physicochemical properties of two pike parvalbumins by means of their intrinsic tyrosyl and phenylalanyl fluorescence. Archives of Biochemistry and Biophysics, 2271: 9-20

Physicochemical properties of 2 pike parvalbumins (pI isoelectric point 5.0 and 4.2), belonging to 2 different gene lineages, were studied by their intrinsic tyrosine and phenylalanine fluorescence. The CD sites of these parvalbumins have similar affinities to Ca2+ (and Mg2+) ions, but the EF sites of the proteins have very different affinities to these ions. This results in differing stabilities of these parvalbumins to pH-, urea- and temperature-induced denaturation. The structure of pike parvalbumin pI 5.0, which binds Ca2+, and Mg2+ ions more tightly, is more stable than that of parvalbumin pI 4.2. Both proteins have higher affinities for Na+ ions than for K+ ions.

US$19.90

PMID: 6639084

DOI: 10.1016/0003-9861(83)90343-0


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