Naslov
Native dimer stabilizes the subunit tertiary structure of porcine class pi glutathione S- transferase

Autori
Erhardt, Julija ; Dirr H.

Izvornik
European journal of biochemistry (0014-2956) 230 (1995), 2; 614-620

Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni

Ključne riječi
glutathione s-transferase ; unfolding ; denaturation ; protein structure

Sažetak
Solvent-induced unfolding of porcine class pi glutathione S-transferase (pGST P1-1), a homodimeric protein, was monitored under equilibrium conditions using different physicochemical parameters (tryptophan fluorescence, anisotropy, degree of tyrosine exposure, binding of 8-anilino-1- naphthalenesulphonic acid, size-exclusion HPLC). The coincidence of unfolding curves obtained with functional (enzyme activity) and structural probes (anisotropy), the absence of thermodynamically stable intermediates such as a folded monomer (determined by binding of 8-anilino-1- naphthalenesulphonic acid and size-exclusion HPLC), and the dependence of pGST P1-1 stability upon protein concentration (measured with structural and functional probes), indicate a cooperative and concerted two-state unfolding transition between native dimeric pGST P1-1 and unfolded monomeric enzyme. [References: 48]

Izvorni jezik
Engleski

Znanstvena područja
Biologija

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