Chaperone-like features of bovine serum albumin: A comparison with α-crystallin

Cellular and Molecular Life Sciences

Volumn 62, Issue 24, 2005, Pages 3092-3099

  Marini, I ^a   Moschini, R ^a   Del Corso, A ^a   Mura, U ^a  

^a UNIVERSITY OF PISA   (Italy)

Author keywords

crystallin; Bovine serum albumin; Enzyme renaturation; Extracellular chaperones; Molecular chaperones; Protein refolding; Sorbitol dehydrogenase

Indexed keywords

ADENOSINE TRIPHOSPHATE; ALPHA CRYSTALLIN; BOVINE SERUM ALBUMIN; CHAPERONE; IDITOL DEHYDROGENASE;

ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; ENZYME INACTIVATION; HEAT; NONHUMAN; PROTEIN AGGREGATION; PROTEIN DENATURATION; PROTEIN FUNCTION;

ALPHA-CRYSTALLINS; ANIMALS; CATTLE; ENZYME ACTIVATION; ENZYME STABILITY; GUANIDINE; L-IDITOL 2-DEHYDROGENASE; MOLECULAR CHAPERONES; PROTEIN DENATURATION; SERUM ALBUMIN, BOVINE; TEMPERATURE; TIME FACTORS;

ANIMALIA; BOVINAE;

EID: 29344458115     PISSN: 1420682X     EISSN: 15691632     Source Type: Journal    
DOI: 10.1007/s00018-005-5397-4     Document Type: Article

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