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. 1989 Jul 1;261(1):189-96.
doi: 10.1042/bj2610189.

The unfolding and refolding of cytoplasmic aspartate aminotransferase from pig heart

S M West  1 , N C Price
Affiliations

The unfolding and refolding of cytoplasmic aspartate aminotransferase from pig heart

S M West et al. Biochem J. .

Abstract

The unfolding of cytoplasmic aspartate aminotransferase from pig heart in solutions of guanidinium chloride (GdnHCl) was studied. Data from protein fluorescence, c.d. and thiol-group reactivity indicated that the enzyme was unfolded in 6 M-GdnHCl. Spectroscopic studies showed that this unfolding was accompanied by dissociation of the pyridoxal 5'-phosphate cofactor. On dilution of the GdnHCl, re-activation of the enzyme occurred in reasonable yield, provided that dithiothreitol and pyridoxal 5'-phosphate were present. The regain of activity obeyed second-order kinetics. In the absence of added dithiothreitol and pyridoxal 5'-phosphate, substantial formation of high-Mr aggregates occurred.

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