Modification of cysteine 111 in human Cu,Zn-superoxide dismutase.

Modification of cysteine 111 in human Cu,Zn-superoxide dismutase. Research Abstract Details 

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Modification of cysteine 111 in human Cu,Zn-superoxide dismutase. Abstract Text:

Ayako Okado-Matsumoto,Ziqiang Guan,Irwin Fridovich,

Human Cu,Zn-superoxide dismutase (hSOD1) has 4 cysteines per subunit. Cys57 and Cys148 are involved in an intrasubunit disulfide bond, while Cys6 and Cys111 are free. Cys6 is buried within the protein while Cys111 is on the surface, near the dimer interface. We examined by liquid chromatography-mass spectrometry the commercially purchased hSOD1 isolated from erythrocytes as well as hSOD1s isolated from human erythrocytes, brain, and hSOD1 expressed in Sf9, yeast, and E. coli. Our goal was to ascertain whether the Cys111 modification occurred naturally in vivo. Only the Sigma erythrocyte hSOD1 appeared to contain a trisulfide crosslink between the Cys111 residues. Thus it failed to react with N-ethylmaleimide, showed absorbtion at 325 nm that was eliminated by 2-mercaptoethanol, and had a mass 30 units more than expected for the native dimer. We examined the possibility that different purification methods might cause this modification in erythrocyte hSOD1. None of the procedures examined for hSOD1 purification produced such a trisulfide. In disagreement with Liu et al. [Biochemistry, 2000, 39, 8125-8132], complete derivitization of both Cys111s of hSOD1 from Sf9 cells with N-ethylmaleimide, 4-vinylpyridine, and by 5,5'-dithiobis(2-nitrobenzoic acid) were readily achieved; indicating that steric hindrance was not a problem.

Modification of cysteine 111 in human Cu,Zn-superoxide dismutase. Publishing Authors By Initials

A Okado-Matsumoto,Z Guan,I Fridovich,

For similar fungi: yeasts research abstracts see: fungi: yeasts research

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Modification of cysteine 111 in human Cu,Zn-superoxide dismutase. Journal Published:

PUBLICATION TYPE: Research Support, N.I.H., Extr

Journal: Free radical biology & medicine

VOLUME: 41

Page Numbers: 1837-46

Journal Abbreviation: Free Radic. Biol. Med.

ISSN: 0891-5849

DAY: 16

MONTH: 09

YEAR: 2006

Modification of cysteine 111 in human Cu,Zn-superoxide dismutase. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 8709159

Modification of cysteine 111 in human Cu,Zn-superoxide dismutase. Keywords Mesh Terms:

KEYWORDS: Yeasts

MESH TERMS: chemistry

Chemical & Substance for Abstract: Modification of cysteine 111 in human Cu,Zn-superoxide dismutase. Information

Substance Name: Superoxide Dismutase

Registry Number: EC 1.15.1.1

Grant and Affiliation Information for Modification of cysteine 111 in human Cu,Zn-superoxide dismutase.

AFFILIATION: Department of Biochemistry, Duke University Medical Center, Durham, NC 27710, USA.

Country: United States

AGENCY: United States NIEHS

GRANT: R21-ES013682

ACRONYM: ES

MEDLINETA: Free Radic Biol Med

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