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Article

Identification of the residues responsible for the alkaline inhibition of the activity of Cu,Zn superoxide dismutase: a study of native and chemically modified enzymes.

Archives of biochemistry and biophysics - 1 Aug 1995

Polticelli F, O'Neill P, Costanzo S, Lania A, Rotilio G, Desideri A

Abstract excerpt

The pH dependence of the activity of Cu,Zn superoxide dismutases from bovine erythrocytes and shark liver was studied by pulse radiolysis in both the native enzymes and those chemically modified at lysine side chains. The study was aimed at identifying the residues responsible for the activity decrease at pH > 9, observed in all native Cu,Zn superoxide dismutases, and is based on the Lys-->Arg substitution...

Topics

Amino Acid Sequence
Animals
Arginine
Binding Sites
Cattle
Erythrocytes
Genetic Variation
Hydrogen-Ion Concentration
Kinetics
Liver
Lysine

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Models, Molecular

Protein Conformation

Sharks

Superoxide Dismutase

Source

Identifiers

PMID: 7639510
DOI: 10.1006/abbi.1995.1376

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-7639510-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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