A simple, rapid and efficient isolation of erythrocyte Cu2Zn2-superoxide dismutase
- 15 July 1984
- journal article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 221 (2) , 549-551
- https://doi.org/10.1042/bj2210549
Abstract
On the basis of the thermal stability of erythrocuprein (Cu2Zn2-superoxide dismutase) a rapid preparation technique was devised and successfully employed to isolate this protein. Partial heat-deterioration of the haemolysate and subsequent chromatography of the supernatant on DEAE-Sephacel and Sephadex G-75 yielded an electrophoretically homogeneous protein within a few days. The physicochemical properties and biochemical function were identical with those reported for Cu2Zn2-superoxide dismutases prepared by established methods.Keywords
This publication has 8 references indexed in Scilit:
- Erythrocuprein (Cu2Zn2 superoxide dismutase) is the major copper protein of the red blood cellFEBS Letters, 1983
- Circular dichroism of metallothioneinsBiochimica et Biophysica Acta (BBA) - Protein Structure, 1978
- Inhibition of nitroblue tetrazolium reduction by cuprein (superoxide dismutase), Cu(tyr)2 and Cu(lys)2FEBS Letters, 1976
- An Enzymic Study on Bovine ErythrocupreinHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1972
- A study on purified bovine erythrocupreinBiochimica et Biophysica Acta (BBA) - Protein Structure, 1971
- Superoxide DismutaseJournal of Biological Chemistry, 1969
- Preparation of Crystalline Erythrocuprein and Catalase from Human ErythrocytesJournal of Biological Chemistry, 1965
- STUDIES ON COPPER METABOLISM .27. ISOLATION AND PROPERTIES OF AN ERYTHROCYTE CUPROPROTEIN (ERYTHROCUPREIN)1959