Opposite behavior of two isozymes when refolding in the presence of non- ionic detergents

Protein Science

Volumn 7, Issue 8, 1998, Pages 1811-1820

  Doñate, Fernando ^a,b   Artigues, Antonio ^a   Iriarte, Ana ^a   Martinez Carrion, Marino ^a  

^a UNIVERSITY OF MISSOURI KANSAS CITY   (United States)

^b SCRIPPS RESEARCH INSTITUTE   (United States)

Author keywords

Chaperonins; Mitochondrial and cytosolic isozymes; Non ionic detergents; Protein refolding intermediates

Indexed keywords

ASPARTATE AMINOTRANSFERASE; BETA CYCLODEXTRIN; CHAPERONIN; DETERGENT; GUANIDINE; ISOENZYME; LUBROL; TRITON X 100; TRYPSIN;

ARTICLE; BINDING AFFINITY; ENZYME ISOLATION; ENZYME REACTIVATION; ENZYME STABILITY; ESCHERICHIA COLI; MICELLE; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ANALYSIS; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN STRUCTURE; STRUCTURE ANALYSIS;

EID: 0032463526     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560070817     Document Type: Article

References (5)

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3. Artigues A, Iriarte A, Martinez-Carrion M. 1997. Refolding intermediates of acid-unfolded mitochondrial aspartate aminotransferase bind to hsp70. J Biol Chem 272:16852-16861.
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5. Clark AC, Frieden C. 1997. GroEL-mediated folding of structurally homologous dihydrofolate reductases. J Mol Biol 268:512-525.