Disruption of the disulfide bonds of recombinant murine interleukin-6 induces formation of a partially unfolded state

Biochemistry

Volumn 36, Issue 9, 1997, Pages 2380-2389

  Zhang, Jian Guo ^b   Matthews, Jacqueline M ^b   Ward, Larry D ^b   Simpson, Richard J ^a,b  

^a ROYAL MELBOURNE HOSPITAL   (Australia)

^b WALTER AND ELIZA HALL INSTITUTE OF MEDICAL RESEARCH   (Australia)

Author keywords

[No Author keywords available]

Indexed keywords

IODOACETAMIDE; IODOACETIC ACID; RECOMBINANT INTERLEUKIN 6;

ARTICLE; CHEMICAL MODIFICATION; CONCENTRATION RESPONSE; CONFORMATIONAL TRANSITION; DENATURATION; DISULFIDE BOND; DRUG CONFORMATION; DRUG STRUCTURE; IMMUNOREGULATION; MOLECULAR INTERACTION; PRIORITY JOURNAL; PROTEIN FOLDING;

ALKYLATION; ANILINO NAPHTHALENESULFONATES; ANIMALS; CHROMATOGRAPHY, GEL; CIRCULAR DICHROISM; CYSTEINE; DISULFIDES; DRUG STABILITY; HYDROGEN-ION CONCENTRATION; INTERLEUKIN-6; METHYLATION; MICE; OXIDATION-REDUCTION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; RECOMBINANT PROTEINS; SPECTROMETRY, FLUORESCENCE; UREA;

MURINAE;

EID: 0031019982     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi962164r     Document Type: Article

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