MOLTEN GLOBULE MONOMERS IN HUMAN SUPEROXIDE-DISMUTASE

被引：21

作者：

SILVA, N

GRATTON, E

MEI, G

ROSATO, N

RUSCH, R

FINAZZIAGRO, A

机构：

[1] UNIV ILLINOIS,DEPT PHYS,FLUORESCENCE DYNAM LAB,URBANA,IL 61801

[2] UNIV ROMA TOR VERGATA,DIPARTIMENTO MED SPERIMENTALE & SCI BIOCHIM,I-00173 ROME,ITALY

[3] BROWN UNIV,DEPT BIOMED,PROVIDENCE,RI 02912

来源：

BIOPHYSICAL CHEMISTRY | 1993年 / 48卷 / 02期

关键词：

HUMAN SUPEROXIDE DISMUTASE; TIME-RESOLVED FLUORESCENCE; GLOBAL ANALYSIS; CONFORMATIONAL SUBSTATES; MOLTEN GLOBULE STATE;

D O I：

10.1016/0301-4622(93)85008-6

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The time-resolved fluorescence decay and anisotropy of Cu/Zn human superoxide dismutase (HSOD) were studied as a function of temperature and denaturant concentration. In addition, circular dichroism (CD) measurements were performed on HSOD as a function of denaturant concentration in the amide and aromatic regions. The time-resolved fluorescence decay results reveal the existence of structural microheterogeneity in HSOD. Furthermore, CD measurements and a global analysis decomposition of the time-resolved fluorescence decay over denaturant concentration shows the presence of an intermediate in the unfolding of HSOD by guanidinium hydrochloride. Considering our previous measurements of partially denatured HSOD as a function of protein concentration (Mei et al., Biochemistry 31 (1992) 7224-7230). our results strongly suggest that the unfolding intermediate is a monomer that displays a molten globule state.

引用

页码：171 / 182

页数：12

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