Use of domain specific ligands to study urea-induced unfolding of bovine serum albumin

Biochemical and Biophysical Research Communications

Volumn 277, Issue 1, 2000, Pages 83-88

  Tayyab, Saad ^a   Sharma, Neeraj ^a   Mushahid Khan, Mohammad ^a  

^a ALIGARH MUSLIM UNIVERSITY   (India)

Author keywords

Bovine serum albumin; Intermediate state; Ligand binding; Urea denaturation

Indexed keywords

BILIRUBIN; BOVINE SERUM ALBUMIN; CHLOROFORM; DIAZEPAM; LIGAND; UREA;

ARTICLE; BINDING AFFINITY; CONFORMATIONAL TRANSITION; DENATURATION; FLUORESCENCE SPECTROSCOPY; FLUOROMETRY; PRIORITY JOURNAL; PROTEIN FOLDING;

BOVINAE;

EID: 0034649231     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1006/bbrc.2000.3642     Document Type: Article

References (16)

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6. Fatty acid binding to bovine serum albumin prevents formation of intermediate during denaturation
7. Refolding of bovine serum albumin and its proteolytic fragments. Regain of disulfide bonds, secondary structure, and ligand-binding ability
8. Anion-induced stabilization of human serum albumin prevents the formation of intermediate during urea denaturation
9. Serum albumin
10. Binding of volatile anesthetic chloroform to albumin demonstrated using tryptophan fluorescence quenching
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13. Use of fluorescence enhancement technique to study bilirubin-albumin interaction
14. Human serum albumin. Spectroscopic studies of binding and proximity relationships for fatty acids and bilirubin
15. Structure of pressure-induced denatured state of human serum albumin. A comparison with the intermediate state in urea-induced denaturation