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Literature DB >> 2775204

The unfolding and refolding of cytoplasmic aspartate aminotransferase from pig heart.

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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Year: 1989 PMID： 2775204 PMCID： PMC1138799 DOI： 10.1042/bj2610189

Source DB: PubMed Journal: Biochem J ISSN： 0264-6021 Impact factor: 3.857

24 in total

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Authors: R Jaenicke
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10. The unfolding and refolding of glutamate dehydrogenases from bovine liver, baker's yeast and Clostridium symbosium.

Authors: S M West; N C Price
Journal: Biochem J Date: 1988-04-01 Impact factor: 3.857

5 in total

1. Biophysical characterization of Entamoeba histolytica phosphoserine aminotransferase (EhPSAT): role of cofactor and domains in stability and subunit assembly.

Authors: Vibhor Mishra; Vahab Ali; Tomoyoshi Nozaki; Vinod Bhakuni
Journal: Eur Biophys J Date: 2010-12-16 Impact factor: 1.733